PBPC_ECOLI
ID PBPC_ECOLI Reviewed; 770 AA.
AC P76577; P76986; P76988;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Penicillin-binding protein 1C;
DE Short=PBP-1c;
DE Short=PBP1c;
DE Includes:
DE RecName: Full=Penicillin-insensitive transglycosylase;
DE EC=2.4.1.129 {ECO:0000269|PubMed:10542235};
DE AltName: Full=Peptidoglycan TGase;
DE Includes:
DE RecName: Full=Transpeptidase-like module;
GN Name=pbpC; Synonyms=yfgN; OrderedLocusNames=b2519, JW2503;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=10542235; DOI=10.1074/jbc.274.45.32031;
RA Schiffer G., Hoeltje J.-V.;
RT "Cloning and characterization of PBP 1C, a third member of the multimodular
RT class A penicillin-binding proteins of Escherichia coli.";
RL J. Biol. Chem. 274:32031-32039(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP REVIEW.
RX PubMed=9841666; DOI=10.1128/mmbr.62.4.1079-1093.1998;
RA Goffin C., Ghuysen J.-M.;
RT "Multimodular penicillin-binding proteins: an enigmatic family of orthologs
RT and paralogs.";
RL Microbiol. Mol. Biol. Rev. 62:1079-1093(1998).
CC -!- FUNCTION: Cell wall formation. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a transpeptidase C-terminal domain which may not be functional.
CC {ECO:0000269|PubMed:10542235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000269|PubMed:10542235};
CC -!- ACTIVITY REGULATION: Transglycosylase activity can be inhibited by
CC moenomycin.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:10542235}; Single-pass type II membrane protein
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Deletion results in an altered mode of murein
CC synthesis. {ECO:0000269|PubMed:10542235}.
CC -!- MISCELLANEOUS: Due to the fact that PBP-1c can neither substitute for
CC PBP-1a or PBP-1b, nor rescue a PBP-1a/PBP-1b double mutant, it is
CC possible that PBP-1c has its own distinct function. Moreover it does
CC not bind to most of the beta-lactams known to bind to other binding
CC proteins, suggesting that the penicillin-binding domain must be
CC different from those present in PBP-1a and PBP-1b. It may function as a
CC transglycosylase only. {ECO:0000269|PubMed:10542235}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000305}.
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DR EMBL; U88571; AAB48052.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75572.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16410.2; -; Genomic_DNA.
DR PIR; F65028; F65028.
DR RefSeq; NP_417014.1; NC_000913.3.
DR RefSeq; WP_001137675.1; NZ_LN832404.1.
DR AlphaFoldDB; P76577; -.
DR SMR; P76577; -.
DR BioGRID; 4260591; 301.
DR DIP; DIP-10442N; -.
DR IntAct; P76577; 9.
DR STRING; 511145.b2519; -.
DR DrugBank; DB01327; Cefazolin.
DR DrugBank; DB09050; Ceftolozane.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PaxDb; P76577; -.
DR PRIDE; P76577; -.
DR EnsemblBacteria; AAC75572; AAC75572; b2519.
DR EnsemblBacteria; BAA16410; BAA16410; BAA16410.
DR GeneID; 947152; -.
DR KEGG; ecj:JW2503; -.
DR KEGG; eco:b2519; -.
DR PATRIC; fig|511145.12.peg.2618; -.
DR EchoBASE; EB3962; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_6; -.
DR InParanoid; P76577; -.
DR OMA; APENFDM; -.
DR PhylomeDB; P76577; -.
DR BioCyc; EcoCyc:G7322-MON; -.
DR BioCyc; MetaCyc:G7322-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P76577; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IDA:EcoliWiki.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:EcoliWiki.
DR GO; GO:0051781; P:positive regulation of cell division; IDA:EcoliWiki.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR02073; PBP_1c; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Hydrolase; Membrane;
KW Multifunctional enzyme; Peptidoglycan synthesis; Protease;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..770
FT /note="Penicillin-binding protein 1C"
FT /id="PRO_0000083188"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..770
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 43..213
FT /note="Transglycosylase"
FT REGION 278..559
FT /note="Transpeptidase"
FT ACT_SITE 84
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 342
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 770 AA; 85067 MW; B227162E5381BEAD CRC64;
MPRLLTKRGC WITLAAAPFL LFLAAWGADK LWPLPLHEVN PARVVVAQDG TPLWRFADAD
GIWRYPVTIE DVSPRYLEAL INYEDRWFWK HPGVNPFSVA RAAWQDLTSG RVISGGSTLT
MQVARLLDPH PKTFGGKIRQ LWRALQLEWH LSKREILTLY LNRAPFGGTL QGIGAASWAY
LGKSPANLSY SEAAMLAVLP QAPSRLRPDR WPERAEAARN KVLERMAVQG VWSREQVKES
REEPIWLAPR QMPQLAPLFS RMMLGKSKSD KITTTLDAGL QRRLEELAQN WKGRLPPRSS
LAMIVVDHTD MRVRGWVGSV DLNDDSRFGH VDMVNSIRSP GSVLKPFVYG LALDEGLIHP
ASLLQDVPRR TGDYRPGNFD SGFHGPISMS EALVRSLNLP AVQVLEAYGP KRFAAKLRNV
GLPLYLPNGA APNLSLILGG AGAKLEDMAA AYTAFARHGK AGKLRLQPDD PLLERPLMSS
GAAWIIRRIM ADEAQPLPDS ALPRVAPLAW KTGTSYGYRD AWAIGVNARY VIGIWTGRPD
GTPVVGQFGF ASAVPLLNQV NNILLSRSAN LPEDPRPNSV TRGVICWPGG QSLPEGDGNC
RRRLATWLLD GSQPPTLLLP EQEGINGIRF PIWLDENGKR VAADCPQARQ EMINVWPLPL
EPWLPASERR AVRLPPASTS CPPYGHDAQL PLQLTGVRDG AIIKRLPGAA EATLPLQSSG
GAGERWWFLN GEPLTERGRN VTLHLTDKGD YQLLVMDDVG QIATVKFVMQ
