ID S6AWP4_PSERE Unreviewed; 780 AA.
AC S6AWP4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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:BAN50808.1};
GN ORFNames=PCA10_50760 {ECO:0000313|EMBL:BAN50808.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN50808.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN50808.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN50808.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
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}.
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DR EMBL; AP013068; BAN50808.1; -; Genomic_DNA.
DR RefSeq; WP_016494935.1; NC_021499.1.
DR AlphaFoldDB; S6AWP4; -.
DR STRING; 1245471.PCA10_50760; -.
DR KEGG; pre:PCA10_50760; -.
DR PATRIC; fig|1245471.3.peg.5150; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_6; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000015503; Chromosome.
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 Glycosyltransferase {ECO:0000313|EMBL:BAN50808.1};
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:UP000015503};
KW Transferase {ECO:0000313|EMBL:BAN50808.1}.
FT DOMAIN 60..226
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 304..520
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 695..776
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 780 AA; 85273 MW; BD4E5DEA008D44BA CRC64;
MKLSSVLRHL RRPWLATPLV LLVLLWAADR LFPLPLPGDD LARVVLAEDG TPLWRFADAE
GVWRYPVNQA EVSPYYLEAL LTYEDRWFYQ HPGVNPLALA RAGWLNLSGG RVLSGGSTLS
MQVARLLDPH PRTFTGKLRQ LWRTAQLEWH LSKDEILGLY LNRAPFGGTL QGVAAASWAY
LGKPPSQLTR ADAALLAVLP QAPSRLRPDR HPERAQAARD KVLRRLAQFQ VWPQSAVQEA
LEEPVLLAPR QEPSLAPLLA RRLNTPASPP LIRTTLDAAL QRRLEDLLLG WRARLPERTS
AAILVVEHET MAVRAYLGSI DIADERRFGH VDMIQALRSP GSTLKPFLYG MALDAGLIHS
ESLLQDVPRR YGDYRPGNFA AGFIGPVSAS EALGMSLNLP AVQLLEAFGP KRFAGELRNV
GVPLALPAAS EPNLALILGG AGSRLEELVS GYSAFARGGR VARLRLQPQD ALQERRLLSP
GSAWIIRRIL AGQARPDRDP RARLTQRPVL AWKTGTSYGF RDAWAIGVGP RHLIGIWIGR
PDGTPVPGQF GLASAAPLLL QVHDLLVNRD AQRGIAAPAD PQPAEVGVAA ICWPLGQPMA
KGDPNCRRQR FAWTLEGTTP PTLLAADQPL GLGLRQPLWV DADGHQVAAG CAGAQARELV
LWPAPLEPWL PRRERRAARL PLPASACPPA LPPPAAPLSI VGVREGDQLR RPAGSADPLR
LKLSTLGGSG RRWWFLDGVP LTATTAEESF NQEFRRSGRH QLSVLDEAGQ TARLEFAVTD
//
