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Penicillin-binding protein 1C (PBP-1c) (PBP1c) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase); Transpeptidase-like module]

 PBPC_ECOLI              Reviewed;         770 AA.
P76577; P76986; P76988;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
05-DEC-2018, entry version 160.
RecName: Full=Penicillin-binding protein 1C;
Short=PBP-1c;
Short=PBP1c;
Includes:
RecName: Full=Penicillin-insensitive transglycosylase;
EC=2.4.1.129 {ECO:0000269|PubMed:10542235};
AltName: Full=Peptidoglycan TGase;
Includes:
RecName: Full=Transpeptidase-like module;
Name=pbpC; Synonyms=yfgN; OrderedLocusNames=b2519, JW2503;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=10542235; DOI=10.1074/jbc.274.45.32031;
Schiffer G., Hoeltje J.-V.;
"Cloning and characterization of PBP 1C, a third member of the
multimodular class A penicillin-binding proteins of Escherichia
coli.";
J. Biol. Chem. 274:32031-32039(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-
K12 genome corresponding to 50.0-68.8 min on the linkage map and
analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
REVIEW.
PubMed=9841666;
Goffin C., Ghuysen J.-M.;
"Multimodular penicillin-binding proteins: an enigmatic family of
orthologs and paralogs.";
Microbiol. Mol. Biol. Rev. 62:1079-1093(1998).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10542235}.
-!- CATALYTIC ACTIVITY:
Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-
D-Ala)](n)-diphospho-di-trans,octa-cis-undecaprenol + beta-D-
GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
diphospho-di-trans,octa-cis-undecaprenol = [GlcNAc-(1->4)-
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-diphospho-
di-trans-octa-cis-undecaprenol + di-trans,octa-cis-undecaprenyl
diphosphate + H(+); Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602,
Rhea:RHEA-COMP:9603, ChEBI:CHEBI:15378, ChEBI:CHEBI:58405,
ChEBI:CHEBI:60033, ChEBI:CHEBI:78435; EC=2.4.1.129;
Evidence={ECO:0000269|PubMed:10542235};
-!- ACTIVITY REGULATION: Transglycosylase activity can be inhibited by
moenomycin.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:10542235}; Single-pass type II membrane
protein {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Deletion results in an altered mode of
murein synthesis. {ECO:0000269|PubMed:10542235}.
-!- 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.
{ECO:0000269|PubMed:10542235}.
-!- SIMILARITY: In the N-terminal section; belongs to the
glycosyltransferase 51 family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
transpeptidase family. {ECO:0000305}.
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EMBL; U88571; AAB48052.1; -; Genomic_DNA.
EMBL; U00096; AAC75572.1; -; Genomic_DNA.
EMBL; AP009048; BAA16410.2; -; Genomic_DNA.
PIR; F65028; F65028.
RefSeq; NP_417014.1; NC_000913.3.
RefSeq; WP_001137675.1; NZ_LN832404.1.
ProteinModelPortal; P76577; -.
SMR; P76577; -.
BioGrid; 4260591; 301.
DIP; DIP-10442N; -.
IntAct; P76577; 9.
STRING; 316385.ECDH10B_2685; -.
DrugBank; DB01327; Cefazolin.
CAZy; GT51; Glycosyltransferase Family 51.
PaxDb; P76577; -.
PRIDE; P76577; -.
EnsemblBacteria; AAC75572; AAC75572; b2519.
EnsemblBacteria; BAA16410; BAA16410; BAA16410.
GeneID; 947152; -.
KEGG; ecj:JW2503; -.
KEGG; eco:b2519; -.
PATRIC; fig|511145.12.peg.2618; -.
EchoBASE; EB3962; -.
EcoGene; EG14210; pbpC.
eggNOG; ENOG4108JQB; Bacteria.
eggNOG; COG4953; LUCA.
HOGENOM; HOG000041141; -.
InParanoid; P76577; -.
KO; K05367; -.
PhylomeDB; P76577; -.
BioCyc; EcoCyc:G7322-MONOMER; -.
BioCyc; MetaCyc:G7322-MONOMER; -.
UniPathway; UPA00219; -.
PRO; PR:P76577; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; ISM:EcoCyc.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0008144; F:drug binding; IDA:EcoCyc.
GO; GO:0008658; F:penicillin binding; IDA:EcoCyc.
GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:EcoCyc.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
GO; GO:0051781; P:positive regulation of cell division; IDA:EcoliWiki.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
Gene3D; 1.10.3810.10; -; 1.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR001264; Glyco_trans_51.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR011815; PBP_1c.
InterPro; IPR009647; PBP_C.
InterPro; IPR036950; PBP_transglycosylase.
InterPro; IPR001460; PCN-bd_Tpept.
Pfam; PF06832; BiPBP_C; 1.
Pfam; PF00912; Transgly; 1.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF56601; SSF56601; 1.
TIGRFAMs; TIGR02073; PBP_1c; 1.
1: Evidence at protein level;
Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
Cell wall biogenesis/degradation; Complete proteome;
Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 770 Penicillin-binding protein 1C.
/FTId=PRO_0000083188.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 770 Periplasmic. {ECO:0000255}.
REGION 43 213 Transglycosylase.
REGION 278 559 Transpeptidase.
ACT_SITE 84 84 Proton donor; for transglycosylase
activity. {ECO:0000250|UniProtKB:P02919}.
ACT_SITE 342 342 Acyl-ester intermediate; for
transpeptidase activity.
{ECO:0000250|UniProtKB:P02919}.
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


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