ID M3H5A9_9LEPT Unreviewed; 693 AA.
AC M3H5A9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 18-JUN-2025, entry version 54.
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:EMF83985.1};
GN ORFNames=LEP1GSC188_4319 {ECO:0000313|EMBL:EMF83985.1};
OS Leptospira weilii serovar Topaz str. LT2116.
OC Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Leptospirales;
OC Leptospiraceae; Leptospira.
OX NCBI_TaxID=1088540 {ECO:0000313|EMBL:EMF83985.1, ECO:0000313|Proteomes:UP000011770};
RN [1] {ECO:0000313|EMBL:EMF83985.1, ECO:0000313|Proteomes:UP000011770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2116 {ECO:0000313|EMBL:EMF83985.1,
RC ECO:0000313|Proteomes:UP000011770};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., Burns M.-A.,
RA Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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=2.4.99.28;
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 -!- 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:EMF83985.1}.
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DR EMBL; AHOR02000010; EMF83985.1; -; Genomic_DNA.
DR AlphaFoldDB; M3H5A9; -.
DR Proteomes; UP000011770; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR FunFam; 3.40.710.10:FF:000111; Penicillin-binding protein 1C; 1.
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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000011770};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 50..209
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 305..579
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 605..689
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 693 AA; 77951 MW; B195965B5F95632C CRC64;
MYKKGIFVFL FISIFFYSNV LSSEEIYSYR EIRDSYHLSD GTILDLHGRF LQTIRLNVRE
RKLAWTEEGE IPETLLLALF AQEDKRFFEH SGVDLIAILG AMKDRVLGNS KRGASTLSMQ
LAGIFLGTKP GRRNIFDKWE QMRFAQKIEQ TWSKNEILTG YLNLIQFRGE HKGLRAASRG
LFQKEPSALS DAESVLLVAM LPFPGASSSA LVKRSCALAK KIQREELCDF FESVVDRMSA
KTGGLPAIEG IAFHAAQKIF RENPEFLSRD GKVKTTLDFD LQWKVTELAK NIIDGLKKQN
VAETGILVLD NLSGAILVYV GNLPDSSSFY VDSISSKRQA GSTLKPFLYG LAFEKEVLKP
NSILEDIPAE WNAVSGIYRP SNYSDTYHGN VQAKYALASS LNIPAIRVLD LVSVQEFVER
LRDLGLSGLK RADFYGSSLA LGSADVTLFE LINAYRTLAN GGMSSRPTFY PYEAKQTLEE
NFREGNFWSR VYTKQAADTL SEILSDREYR SLSFGLNNHL STRFFTAVKT GTSQDMRDNW
CVGYSKNYTV GVWVGNMNGS PMWDVSGVTG AAPIWNAVMS LLQEREKQPG NTFFGTFSDL
HVRQLAQSSS IPKILIPGNE TIYALDPDIP EGRQKLYFSA SAFMSGFRWV LDGKRIQEAK
QKNVFWKPER GFHILSLQDK DGKIIDSVVF EVR
//
