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Protein

Penicillin-binding protein 1C

Gene

pbpC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional.1 Publication

Miscellaneous

Due to the fact that PBP-1c can neither substitute for PBP-1a or PBP-1b, nor rescue a PBP-1a/PBP-1b double mutant, it is possible that PBP-1c has its own distinct function. Moreover it does not bind to most of the beta-lactams known to bind to other binding proteins, suggesting that the penicillin-binding domain must be different from those present in PBP-1a and PBP-1b. It may function as a transglycosylase only.1 Publication

Catalytic activityi

(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate.1 Publication

Enzyme regulationi

Transglycosylase activity can be inhibited by moenomycin.

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei84Proton donor; for transglycosylase activityBy similarity1
Active sitei342Acyl-ester intermediate; for transpeptidase activityBy similarity1

GO - Molecular functioni

  • carboxypeptidase activity Source: UniProtKB-KW
  • drug binding Source: EcoCyc
  • penicillin binding Source: EcoCyc
  • peptidoglycan glycosyltransferase activity Source: EcoCyc

GO - Biological processi

Keywordsi

Molecular functionCarboxypeptidase, Glycosyltransferase, Hydrolase, Protease, Transferase
Biological processCell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciEcoCyc:G7322-MONOMER.
MetaCyc:G7322-MONOMER.
UniPathwayiUPA00219.

Protein family/group databases

CAZyiGT51. Glycosyltransferase Family 51.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin-binding protein 1C
Short name:
PBP-1c
Short name:
PBP1c
Including the following 2 domains:
Penicillin-insensitive transglycosylase (EC:2.4.1.1291 Publication)
Alternative name(s):
Peptidoglycan TGase
Transpeptidase-like module
Gene namesi
Name:pbpC
Synonyms:yfgN
Ordered Locus Names:b2519, JW2503
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14210. pbpC.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 8CytoplasmicSequence analysis8
Transmembranei9 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini30 – 770PeriplasmicSequence analysisAdd BLAST741

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Deletion results in an altered mode of murein synthesis.1 Publication

Chemistry databases

DrugBankiDB01327. Cefazolin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000831881 – 770Penicillin-binding protein 1CAdd BLAST770

Proteomic databases

PaxDbiP76577.
PRIDEiP76577.

Interactioni

Protein-protein interaction databases

BioGridi4260591. 250 interactors.
DIPiDIP-10442N.
IntActiP76577. 9 interactors.
MINTiMINT-1308552.
STRINGi316385.ECDH10B_2685.

Structurei

3D structure databases

ProteinModelPortaliP76577.
SMRiP76577.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni43 – 213TransglycosylaseAdd BLAST171
Regioni278 – 559TranspeptidaseAdd BLAST282

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyltransferase 51 family.Curated
In the C-terminal section; belongs to the transpeptidase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108JQB. Bacteria.
COG4953. LUCA.
HOGENOMiHOG000041141.
InParanoidiP76577.
KOiK05367.
PhylomeDBiP76577.

Family and domain databases

Gene3Di1.10.3810.10. 1 hit.
InterProiView protein in InterPro
IPR012338. Beta-lactam/transpept-like.
IPR001264. Glyco_trans_51.
IPR023346. Lysozyme-like_dom.
IPR011815. PBP_1c.
IPR009647. PBP_C.
IPR001460. PCN-bd_Tpept.
PfamiView protein in Pfam
PF06832. BiPBP_C. 1 hit.
PF00912. Transgly. 1 hit.
PF00905. Transpeptidase. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF56601. SSF56601. 1 hit.
TIGRFAMsiTIGR02073. PBP_1c. 1 hit.

Sequencei

Sequence statusi: Complete.

P76577-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRLLTKRGC WITLAAAPFL LFLAAWGADK LWPLPLHEVN PARVVVAQDG
60 70 80 90 100
TPLWRFADAD GIWRYPVTIE DVSPRYLEAL INYEDRWFWK HPGVNPFSVA
110 120 130 140 150
RAAWQDLTSG RVISGGSTLT MQVARLLDPH PKTFGGKIRQ LWRALQLEWH
160 170 180 190 200
LSKREILTLY LNRAPFGGTL QGIGAASWAY LGKSPANLSY SEAAMLAVLP
210 220 230 240 250
QAPSRLRPDR WPERAEAARN KVLERMAVQG VWSREQVKES REEPIWLAPR
260 270 280 290 300
QMPQLAPLFS RMMLGKSKSD KITTTLDAGL QRRLEELAQN WKGRLPPRSS
310 320 330 340 350
LAMIVVDHTD MRVRGWVGSV DLNDDSRFGH VDMVNSIRSP GSVLKPFVYG
360 370 380 390 400
LALDEGLIHP ASLLQDVPRR TGDYRPGNFD SGFHGPISMS EALVRSLNLP
410 420 430 440 450
AVQVLEAYGP KRFAAKLRNV GLPLYLPNGA APNLSLILGG AGAKLEDMAA
460 470 480 490 500
AYTAFARHGK AGKLRLQPDD PLLERPLMSS GAAWIIRRIM ADEAQPLPDS
510 520 530 540 550
ALPRVAPLAW KTGTSYGYRD AWAIGVNARY VIGIWTGRPD GTPVVGQFGF
560 570 580 590 600
ASAVPLLNQV NNILLSRSAN LPEDPRPNSV TRGVICWPGG QSLPEGDGNC
610 620 630 640 650
RRRLATWLLD GSQPPTLLLP EQEGINGIRF PIWLDENGKR VAADCPQARQ
660 670 680 690 700
EMINVWPLPL EPWLPASERR AVRLPPASTS CPPYGHDAQL PLQLTGVRDG
710 720 730 740 750
AIIKRLPGAA EATLPLQSSG GAGERWWFLN GEPLTERGRN VTLHLTDKGD
760 770
YQLLVMDDVG QIATVKFVMQ
Length:770
Mass (Da):85,067
Last modified:February 1, 1997 - v1
Checksum:iB227162E5381BEAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88571 Genomic DNA. Translation: AAB48052.1.
U00096 Genomic DNA. Translation: AAC75572.1.
AP009048 Genomic DNA. Translation: BAA16410.2.
PIRiF65028.
RefSeqiNP_417014.1. NC_000913.3.
WP_001137675.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75572; AAC75572; b2519.
BAA16410; BAA16410; BAA16410.
GeneIDi947152.
KEGGiecj:JW2503.
eco:b2519.
PATRICifig|511145.12.peg.2618.

Similar proteinsi

Entry informationi

Entry nameiPBPC_ECOLI
AccessioniPrimary (citable) accession number: P76577
Secondary accession number(s): P76986, P76988
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: August 30, 2017
This is version 153 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families