Penicillin-binding protein 1A - Escherichia coli (strain K12)

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P02918 (PBPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 136. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Penicillin-binding protein 1A
Short name=PBP-1a
Short name=PBP1a

Including the following 2 domains:

Penicillin-insensitive transglycosylase
EC=2.4.2.-
Alternative name(s):
Peptidoglycan TGase
Penicillin-sensitive transpeptidase
EC=3.4.-.-
Alternative name(s):
DD-transpeptidase

Gene names

Name:	mrcA
Synonyms:	ponA
Ordered Locus Names:	b3396, JW3359

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	850 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular location	Cell inner membrane; Single-pass type II membrane protein By similarity.
Sequence similarities	In the N-terminal section; belongs to the glycosyltransferase 51 family. In the C-terminal section; belongs to the transpeptidase family.
Sequence caution	The sequence AAA58193.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Antibiotic resistance Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Hydrolase Transferase
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of cytolysis Inferred from genetic interaction PubMed 7027927. Source: EcoCyc peptidoglycan biosynthetic process Inferred from direct assay PubMed 16840781. Source: EcoCyc regulation of cell shape Inferred from genetic interaction PubMed 7007327 PubMed 9324260. Source: EcoCyc response to antibiotic Inferred from mutant phenotype PubMed 330236. Source: EcoCyc
Cellular_component	integral to plasma membrane Inferred from direct assay PubMed 319999. Source: EcoliWiki peptidoglycan-based cell wall Inferred from electronic annotation. Source: InterPro
Molecular_function	penicillin binding Inferred from direct assay PubMed 330236. Source: EcoCyc peptidoglycan glycosyltransferase activity Inferred from direct assay PubMed 16840781. Source: EcoCyc serine-type D-Ala-D-Ala carboxypeptidase activity Inferred from direct assay PubMed 16840781. Source: EcoCyc transferase activity, transferring pentosyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
lpoA	P45464	4	EBI-1126191,EBI-557795

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 850

850

Penicillin-binding protein 1A

PRO_0000083164

Regions

Topological domain

1 – 5

Cytoplasmic Potential

Transmembrane

6 – 26

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

27 – 850

824

Periplasmic Potential

Region

48 – 216

169

Transglycosylase

Region

400 – 710

311

Transpeptidase

Sites

Active site

Proton donor; for transglycosylase activity Potential

Active site

465

Acyl-ester intermediate; for transpeptidase activity

Sequences

Sequence

Length

Mass (Da)

Tools

P02918 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0A54C6B28783E34B
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FASTA

850

93,636

        10         20         30         40         50         60 
MKFVKYFLIL AVCCILLGAG SIYGLYRYIE PQLPDVATLK DVRLQIPMQI YSADGELIAQ 

        70         80         90        100        110        120 
YGEKRRIPVT LDQIPPEMVK AFIATEDSRF YEHHGVDPVG IFRAASVALF SGHASQGAST 

       130        140        150        160        170        180 
ITQQLARNFF LSPERTLMRK IKEVFLAIRI EQLLTKDEIL ELYLNKIYLG YRAYGVGAAA 

       190        200        210        220        230        240 
QVYFGKTVDQ LTLNEMAVIA GLPKAPSTFN PLYSMDRAVA RRNVVLSRML DEGYITQQQF 

       250        260        270        280        290        300 
DQTRTEAINA NYHAPEIAFS APYLSEMVRQ EMYNRYGESA YEDGYRIYTT ITRKVQQAAQ 

       310        320        330        340        350        360 
QAVRNNVLDY DMRHGYRGPA NVLWKVGESA WDNNKITDTL KALPTYGPLL PAAVTSANPQ 

       370        380        390        400        410        420 
QATAMLADGS TVALSMEGVR WARPYRSDTQ QGPTPRKVTD VLQTGQQIWV RQVGDAWWLA 

       430        440        450        460        470        480 
QVPEVNSALV SINPQNGAVM ALVGGFDFNQ SKFNRATQAL RQVGSNIKPF LYTAAMDKGL 

       490        500        510        520        530        540 
TLASMLNDVP ISRWDASAGS DWQPKNSPPQ YAGPIRLRQG LGQSKNVVMV RAMRAMGVDY 

       550        560        570        580        590        600 
AAEYLQRFGF PAQNIVHTES LALGSASFTP MQVARGYAVM ANGGFLVDPW FISKIENDQG 

       610        620        630        640        650        660 
GVIFEAKPKV ACPECDIPVI YGDTQKSNVL ENNDVEDVAI SREQQNVSVP MPQLEQANQA 

       670        680        690        700        710        720 
LVAKTGAQEY APHVINTPLA FLIKSALNTN IFGEPGWQGT GWRAGRDLQR RDIGGKTGTT 

       730        740        750        760        770        780 
NSSKDAWFSG YGPGVVTSVW IGFDDHRRNL GHTTASGAIK DQISGYEGGA KSAQPAWDAY 

       790        800        810        820        830        840 
MKAVLEGVPE QPLTPPPGIV TVNIDRSTGQ LANGGNSREE YFIEGTQPTQ QAVHEVGTTI 

       850 
IDNGEAQELF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12." Broome-Smith J.K., Edelman A., Yousif S., Spratt B.G. Eur. J. Biochem. 147:437-446(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12." Keck W., Glauner B., Schwarz U., Broome-Smith J.K., Spratt B.G. Proc. Natl. Acad. Sci. U.S.A. 82:1999-2003(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 452-480. Strain: K12.
[5]	"Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A." Ishino F., Mitsui K., Tamaki S., Matsuhashi M. Biochem. Biophys. Res. Commun. 97:287-293(1980) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: K12.
[6]	"Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs." Goffin C., Ghuysen J.-M. Microbiol. Mol. Biol. Rev. 62:1079-1093(1998) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X02164 Genomic DNA. Translation: CAA26100.1. U18997 Genomic DNA. Translation: AAA58193.1. Different initiation. U00096 Genomic DNA. Translation: AAC76421.2. AP009048 Genomic DNA. Translation: BAE77895.1.
PIR	ZPECPA. G65134.
RefSeq	NP_417855.4. NC_000913.2. YP_492036.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P02918.
SMR	P02918. Positions 47-789.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10251N.
IntAct	P02918. 8 interactions.
STRING	511145.b3396.
Protein family/group databases
CAZy	GT51. Glycosyltransferase Family 51.
Proteomic databases
PaxDb	P02918.
PRIDE	P02918.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76421; AAC76421; b3396. BAE77895; BAE77895; BAE77895.
GeneID	12933998. 947907.
KEGG	ecj:Y75_p3780. eco:b3396.
PATRIC	32122224. VBIEscCol129921_3489.
Organism-specific databases
EchoBASE	EB0741.
EcoGene	EG10748. mrcA.
Phylogenomic databases
eggNOG	COG5009.
HOGENOM	HOG000041138.
KO	K05366.
OMA	REIGANG.
ProtClustDB	PRK11636.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10748-MONOMER. ECOL316407:JW3359-MONOMER. MetaCyc:EG10748-MONOMER.
UniPathway	UPA00219.
Gene expression databases
Genevestigator	P02918.
Family and domain databases
Gene3D	2.40.50.140. 1 hit. 3.40.710.10. 3 hits.
InterPro	IPR012338. Beta-lactam/transpept-like. IPR001264. Glyco_trans_51. IPR012340. NA-bd_OB-fold. IPR011816. PBP_1a. IPR001460. PCN-bd_Tpept. [Graphical view]
Pfam	PF00912. Transgly. 1 hit. PF00905. Transpeptidase. 1 hit. [Graphical view]
SUPFAM	SSF56601. PBP_transp_fold. 1 hit.
TIGRFAMs	TIGR02074. PBP_1a_fam. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL1813.
DrugBank	DB01413. Cefepime. DB00303. Ertapenem.

Entry information

Entry name

PBPA_ECOLI

Accession

Primary (citable) accession number: P02918
Secondary accession number(s): P76688, Q2M761

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents