RegulonDB

Gene
Name:	mrcB
Synonym(s):	ECK0148, EG10605, b0149, pbpF, ponB
Genome position(nucleotides):	164730 --> 167264
Strand:	forward
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	55.15
External database links:

ASAP:	ABE-0000516
CGSC:	483
ECHOBASE:	EB0600
ECOLIHUB:	mrcB
OU-MICROARRAY:	b0149
STRING:	511145.b0149
COLOMBOS:	mrcB

Gene

Name:

mrcB

Synonym(s):

ECK0148, EG10605, b0149, pbpF, ponB

Genome position(nucleotides):

164730 --> 167264

Strand:

forward

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

55.15

External database links:

ASAP:

CGSC:

ECHOBASE:

ECOLIHUB:

OU-MICROARRAY:

STRING:

COLOMBOS:

Type

Positions

Sequence

Comment

1 -> 79

MAGNDREPIGRKGKPTRPVKQKVSRRRYEDDDDYDDYDDYEDEEPMPRKGKGKGKGRKPRGKRGWLWLLLKLAIVFAVL

64 -> 87

GWLWLLLKLAIVFAVLIAIYGVYL

UniProt: Helical; Signal-anchor for type II membrane protein.

88 -> 250

DQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTISKNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHLATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGR

UniProt: Membrane association; Sequence Annotation Type: region of interest.

103 -> 103

UniProt: In Ref. 1 and 2..

109 -> 109

R → G: decreased functionality - loss of fitness in a ΔmrcA background; purified protein has decreased basal glycosyltransferase and transpeptidase activity; decreased affinity for LpoB

Type

Positions

Sequence

Comment

1 -> 79

MAGNDREPIGRKGKPTRPVKQKVSRRRYEDDDDYDDYDDYEDEEPMPRKGKGKGKGRKPRGKRGWLWLLLKLAIVFAVL

64 -> 87

GWLWLLLKLAIVFAVLIAIYGVYL

UniProt: Helical; Signal-anchor for type II membrane protein.

88 -> 250

DQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTISKNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHLATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGR

UniProt: Membrane association; Sequence Annotation Type: region of interest.

103 -> 103

UniProt: In Ref. 1 and 2..

109 -> 109

R → G: decreased functionality - loss of fitness in a ΔmrcA background; purified protein has decreased basal glycosyltransferase and transpeptidase activity; decreased affinity for LpoB

112 -> 112

N → G: purified protein has increased basal transpeptidase and glycosyltransferase activity; increased affinity for LpoB

113 -> 197

LEPDMTISKNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHLATIVNMENNRQFGFFRL

134 -> 134

R → E: decreased functionality - loss of fitness in a ΔmrcA background; purified protein has increased basal glycosyltransferase and transpeptidase activity

157 -> 157

R → A: decreased functionality - loss of fitness in a ΔmrcA background; purified protein has decreased basal glycosyltransferase and transpeptidase activity; impacts (negatively) LpoB-mediated stimulation of glycosyltransferase activity

195 -> 367

FRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDARYSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASIYNPWRNPK

UniProt: Transglycosylase; Sequence Annotation Type: region of interest.

196 -> 196

R → G: decreased functionality - loss of fitness in a ΔmrcA background

198 -> 198

D → A: decreased functionality - loss of fitness in a ΔmrcA background; purified protein has increased basal glycosyltransferase activity; impacts (negatively) LpoB-mediated stimulation of glycosyltransferase activity

202 -> 202

I → F: does not require the presence of LpoB for activity in vivo (at 30 °C only); elevated peptidoglycan glycosyltransferase activity in vitro.

209 -> 380

NGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDARYSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASIYNPWRNPKLALERRNLVLRLL

233 -> 242

EDRHFYEHDG

Glycosyl transferase domain, conserved motif 1

234 -> 234

UniProt: 7-fold decrease in catalytic activity. No complementation in strain defective in PBP-1b..

264 -> 271

GASTLTQQ

Glycosyl transferase domain, conserved motif 2

286 -> 290

RKANE

Glycosyl transferase domain, conserved motif 3

290 -> 290

UniProt: 11-fold decrease in catalytic activity. Shows complementation activity in strain defective in PBP-1b..

303 -> 312

KDRILELYMN

Glycosyl transferase domain, conserved motif 4

313 -> 313

E → D: does not require the presence of LpoB for activity in vivo; elevated peptidoglycan glycosyltransferase activity in vitro.

318 -> 318

Q → A: decreased functionality - loss of fitness in a ΔmrcA background; purified protein has decreased basal glycosyltransferase activity; impacts (positively) LpoB-mediated stimulation of glycosyltransferase activity and (negatively) LpoB-mediated stimulation of transpeptidase activity; produces glycan chains with a significantly decreased average length (~8 disaccharide units)

341 -> 341

E → A: decreased functionality - loss of fitness in a ΔmrcA background; purified protein has decreased basal glycosyltransferase and transpeptidase activity; impacts (negatively) LpoB-mediated stimulation of glycosyltransferase acitvity; increased affinity for LpoB

355 -> 355

K → A: decreased functionality - loss of fitness in a ΔmrcA background; purified protein has decreased basal glycosyltransferase activity and increased basal transpeptidase activity; impacts (positively) LpoB-mediated stimulation of glycosyltransferase activity

372 -> 377

RRNLVL

Glycosyl transferase domain, conserved motif 5

411 -> 411

Q → R: does not require the presence of LpoB for activity in vivo; elevated peptidoglycan glycosyltransferase activity in vitro.

435 -> 447

GVKIFTTFDSVAQ

junction between the glycosyl transferase and acyl transferase modules of PBP1B

437 -> 437

K → A: decreased functionality - loss of fitness in a ΔmrcA background; purified protein has decreased basal glycosyltransferase activity; impacts (positively) LpoB-mediated stimulation of glycosyltransferase activity

443 -> 443

D → A: purified protein has increased basal glycosyltransferase and transpeptidase activity; enhances stimulatory effect of LpoB; increased affinity for LpoB

444 -> 736

SVAQDAAEKAAVEGIPALKKQRKLSDLETAIVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIALRQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPKDQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAERAVPAQAAYLTLWTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTNNNVDTWFAGIDGSTVTITWVGRDNNQPTKLYGA

UniProt: Transpeptidase; Sequence Annotation Type: region of interest.

473 -> 714

AIVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIALRQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPKDQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAERAVPAQAAYLTLWTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTNNNVDTWFAGID

510 -> 513

SLAK

Acyll transferase domain, conserved motif 7

572 -> 574

SMN

Acyl transferase domain, conserved motif 8

698 -> 700

KTG

Acyl transferase domain, conserved motif 9

754 -> 754

UniProt: In Ref. 2..

793 -> 828

LCQQSEMQQQPSGNPFDQSSQPQQQPQQQPAQQEQK

UniProt: Polar residues; Sequence Annotation Type: compositionally biased region.

68 -> 152

LLLKLAIVFAVLIAIYGVYLDQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTISKNEMVKLLEATQYRQVSKMTRPGEFTVQANSI

164 -> 335

SKEGQVRARLTFDGDHLATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDARYSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYF

428 -> 669

DKVKDLSGVKIFTTFDSVAQDAAEKAAVEGIPALKKQRKLSDLETAIVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIALRQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPKDQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAERAVPAQAAYL

Multifun Terms (GenProtEC)

1 - metabolism --> 1.6 - biosynthesis of macromolecules (cellular constituents) --> 1.6.7 - murein (peptidoglycan)

1 - metabolism --> 1.7 - central intermediary metabolism --> 1.7.12 - amino sugar conversions

5 - cell processes --> 5.1 - cell division

5 - cell processes --> 5.6 - protection --> 5.6.4 - drug resistance/sensitivity

6 - cell structure --> 6.2 - murein

1 - metabolism --> 1.6 - biosynthesis of macromolecules (cellular constituents) --> 1.6.7 - murein (peptidoglycan)

1 - metabolism --> 1.7 - central intermediary metabolism --> 1.7.12 - amino sugar conversions

5 - cell processes --> 5.1 - cell division

5 - cell processes --> 5.6 - protection --> 5.6.4 - drug resistance/sensitivity

6 - cell structure --> 6.2 - murein

Gene Ontology Terms (GO)

cellular_component

GO:0016020 - membrane
GO:0030288 - outer membrane-bounded periplasmic space
GO:0005886 - plasma membrane
GO:0005887 - integral component of plasma membrane
GO:0016021 - integral component of membrane
GO:0009274 - peptidoglycan-based cell wall

molecular_function

GO:0003824 - catalytic activity
GO:0005515 - protein binding
GO:0016757 - glycosyltransferase activity
GO:0008233 - peptidase activity
GO:0016787 - hydrolase activity
GO:0016740 - transferase activity
GO:0004180 - carboxypeptidase activity
GO:0008955 - peptidoglycan glycosyltransferase activity
GO:0009002 - serine-type D-Ala-D-Ala carboxypeptidase activity
GO:0008658 - penicillin binding
GO:0071723 - lipopeptide binding

biological_process

GO:0010165 - response to X-ray
GO:0051518 - positive regulation of bipolar cell growth
GO:0071433 - cell wall repair
GO:0008152 - metabolic process
GO:0006508 - proteolysis
GO:0009252 - peptidoglycan biosynthetic process
GO:0046677 - response to antibiotic
GO:0008360 - regulation of cell shape
GO:0071555 - cell wall organization

	Type	Name	Post Left	Post Right	Strand	Notes	Evidence (Confirmed, Strong, Weak)	References
	promoter	TSS_288	164658		forward	nd	[RS-EPT-CBR]	[2]

Type

Name

Post Left

Post Right

Strand

Notes

Evidence (Confirmed, Strong, Weak)

References

promoter

TSS_288

164658

forward

[RS-EPT-CBR]

[2]

Evidence
[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Evidence

[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Reference(s)
[1] de la Rosa EJ., de Pedro MA., Vazquez D., 1985, Penicillin binding proteins: role in initiation of murein synthesis in Escherichia coli., Proc Natl Acad Sci U S A 82(17):5632-5
[2] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

Reference(s)

[1] de la Rosa EJ., de Pedro MA., Vazquez D., 1985, Penicillin binding proteins: role in initiation of murein synthesis in Escherichia coli., Proc Natl Acad Sci U S A 82(17):5632-5

[2] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.