ID A0A430KQ35_9GAMM Unreviewed; 778 AA.
AC A0A430KQ35;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpC {ECO:0000313|EMBL:RTE65617.1};
GN ORFNames=EH243_11800 {ECO:0000313|EMBL:RTE65617.1};
OS Amphritea opalescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Amphritea.
OX NCBI_TaxID=2490544 {ECO:0000313|EMBL:RTE65617.1, ECO:0000313|Proteomes:UP000283087};
RN [1] {ECO:0000313|EMBL:RTE65617.1, ECO:0000313|Proteomes:UP000283087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANRC-JH13 {ECO:0000313|EMBL:RTE65617.1,
RC ECO:0000313|Proteomes:UP000283087};
RA Fang Z., Zhang Y., Han X.;
RT "The draft genome sequence of Amphritea opalescens ANRC-JH13T.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RTE65617.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RQXW01000009; RTE65617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430KQ35; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000283087; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 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 NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000283087}.
FT DOMAIN 55..221
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 303..558
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 690..774
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 778 AA; 86562 MW; DF6F72183752C8F2 CRC64;
MLRLFSKRRA VYAGLLVLLA GATLWWPLPK PLFNQPLSRL LLDQQQQLLS ARIAADQQWR
FKSVASLSPA YQTALIQYED KRFMQHPGVD PLAILRALYL NLKSGRVVSG GSTITMQLAR
MVEGNQPRTL WQKLQELHLA LRLEVQLTKA EILSLYAANA PMGGNTVGID AAAWRYFGRS
LAELSWAEAA LLAVLPNNPA AMHLSRSRDK LQAKRDFLLH KLWLKGILTE QDYRLSLLES
IPQRPRRWPS YGQHLLDRLS QQYPDQSVFY TSIDRRLTQK IEFITRQHSQ RLGAIGIHNL
ALLVVDNASM QVKAYFGNVA YSDRPEDGSH VDIASRPRSS GSTLKPFLYA AMLDNGDITP
QTLIPDVPTA YGSYQPSNYD QSFRGAVTAR SALTASLNIP SVRMLNDYSY QAFYDKLQAL
GFSNLFRQPD EYGLSLILGG AEVSLVDLTA AYAGLSRRAQ QAAPLSFEAL NYGVSFDHEK
AEKTAYPLSQ GAAWLTLDAL SDVTRPGLHK IHRLFSGSAR VAWKTGTSYG LRDGWAVGTT
ENVTVGVWVG NANGEGRQLL TGTSAAAPVL FDTLNIINDL GWPEEPSGAL KSIEVCRENG
FLPKFGCPRE RVTIPAAAQF EKVSPHHFQV TVDRNTGLRS SIGCNPTGSI ISKTFFQLPP
SQAAFYRIAH ASYHPVPEFD EGCTPDRRAL NGRFEVTYPR AGQIISLPRY MSGQPGEVIF
RATAKSDSAQ LFWHLDKHYL GATKTFHELS ETLQPGKHLL RVVDQQGVWQ QIRFTVIP
//