ID Q92VA7_RHIME Unreviewed; 713 AA.
AC Q92VA7;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 18-JUN-2025, entry version 124.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN Name=pbpC {ECO:0000313|EMBL:CAC49201.1};
GN ORFNames=SM_b21297 {ECO:0000313|EMBL:CAC49201.1};
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB {ECO:0000313|EMBL:CAC49201.1,
OG ECO:0000313|Proteomes:UP000001976}.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834 {ECO:0000313|EMBL:CAC49201.1, ECO:0000313|Proteomes:UP000001976};
RN [1] {ECO:0000313|EMBL:CAC49201.1, ECO:0000313|Proteomes:UP000001976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021 {ECO:0000313|EMBL:CAC49201.1,
RC ECO:0000313|Proteomes:UP000001976};
RC PLASMID=Plasmid pSymB {ECO:0000313|Proteomes:UP000001976};
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorholter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puhler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2] {ECO:0000313|Proteomes:UP000001976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021 {ECO:0000313|Proteomes:UP000001976};
RC PLASMID=Plasmid pSymB {ECO:0000313|Proteomes:UP000001976};
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
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 ---------------------------------------------------------------------------
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; AL591985; CAC49201.1; -; Genomic_DNA.
DR PIR; A95942; A95942.
DR RefSeq; NP_437341.1; NC_003078.1.
DR RefSeq; WP_010975657.1; NC_003078.1.
DR AlphaFoldDB; Q92VA7; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; CAC49201; CAC49201; SM_b21297.
DR KEGG; sme:SM_b21297; -.
DR PATRIC; fig|266834.11.peg.5731; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_5; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:InterPro.
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; IPR050396; Glycosyltr_51/Transpeptidase.
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:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Plasmid {ECO:0000313|EMBL:CAC49201.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001976};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 80..246
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 324..540
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 624..710
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 713 AA; 76970 MW; 3E6C00A6F0443A5D CRC64;
MMFSRRKSYR NGIVPAPRLP SGRGRAIVAL SLALILSALA VFTLEWADRT FPPPLSEADT
VSAEVLDRDG RLLRAFAAKD GLWRLKTTAQ DVDPRFIEML IAYEDQRFRE HHGVDPLALA
RAALQFVTNG RIVSGASTLS MQVARLIEPR ERRTLGAKLL QVARAIQIER RLGKDEILDL
YLTHAPYGGN LEGVRAASLA WFGKEPRRLS AGEAALLVAL PQLPEKRRPD RNLAAAEAAR
KRVLARAAVA RVIGEGEAER AAMTAIPTRR LQLPAHAAHL AEAARRKDPA GRRHPTTLSR
NIQRSLEGVA REGAARLGPK VSVAMVMADI RTGEIVGEVG SADYFDASRS GWIDMSRITR
SPGSTLKPFI YGLAFEEGLV SQETIIEDRP ADFFGYRPRN FDMNYQGDVT VRQALQLSLN
VPAIRLLDAV GPSRLMVRFR RADVRPKLPP HEAPGLAIGL GGVGITLHEL VQLYAGLANQ
GWPVRLGDGI EGVPGPTDGE PLLSTVAAWH VADILSDVLP PAGSRRHGIA YKTGTSYGYR
DAWSVGFDGR YVLGVWVGRP DNGAVPGLTG YGAAAPILFE GFAKAGIAIT PLPGPPAGAV
RLVQADLPIS QRRFSVTANG LLSASVREAA PQIVFPPEGA RVELGAQGDG VITPLTLKLQ
GGRAPFRWLA NGRPLPDVAR RRVSQWQPDG GGYSTLTVID ALGRAASVRV FVQ
//
