ID A0A3M2HN14_9GAMM Unreviewed; 793 AA.
AC A0A3M2HN14;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:RMH91096.1};
GN ORFNames=EBB59_08100 {ECO:0000313|EMBL:RMH91096.1};
OS Lysobacter pythonis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=2483112 {ECO:0000313|EMBL:RMH91096.1, ECO:0000313|Proteomes:UP000275012};
RN [1] {ECO:0000313|EMBL:RMH91096.1, ECO:0000313|Proteomes:UP000275012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4284/11 {ECO:0000313|EMBL:RMH91096.1,
RC ECO:0000313|Proteomes:UP000275012};
RA Hans-Juergen B., Huptas C., Sandra B., Igor L., Joachim S., Siegfried S.,
RA Mareike W., Peter K.;
RT "Proposal of Lysobacter pythonis sp. nov. isolated from royal pythons
RT (Python regius).";
RL Submitted (OCT-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:RMH91096.1}.
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DR EMBL; RFLY01000010; RMH91096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2HN14; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000275012; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000275012};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..235
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 313..529
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 703..785
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 793 AA; 86022 MW; 155A7DA6B8F660EC CRC64;
MKGDSDSPAG VVLPRHRVLR ALAIALCLLV LVVLTLDRLF PLPLPRRGDM SVLVTARDGR
PLRAFADAGG VWRHPATPDT VSPLYLEALL GYEDRWFWRH PGINPFALGR AGWQVLRAGR
IVSGGSTLTM QVARLIDPHS RSLGGKFKQM LRALQLEAHL SKREILTLYL ERAPYGGVIE
GVDTASWAYL GKPASELSHA EAALLAVLPQ SPSRLRPDRA PEAARRARDK LLARMAALGL
WTEAEVEDAR IEPVVARSLQ PPLVAALLAE RLRREHPGEA RIVSTLDIDL QRALEARVRG
YFARLPPRTS AALLVIDNRT MEARAYVGSV AYGDKARLGH IDMVRAVRSP GSTLKPFLYG
LALDDGLIHS ESLFVDAPQA FGGYRPGNFG EDFHGPVSAA DALRMSLNVP AVALLEQVGP
ARFAARLDNA GLALRLPAGA KPNLAMILGG VGTRLDDLLG AYAALQRGGV AGRVRYVAGD
RRRERRLLSP GAAWIVREML QANPRPGAVM GVSASRHPVA WKTGTSYGYR DAWALGSTPD
YSVGLWVGRP DGTPLPGQYG AVTALPLMFE VIDTLPRPRR SPPSTVRPID VEAATICWPL
GTAPEPAAPA LCRQRRQAWI LNGGIPPTFP ERESRGWNSL RERLRVDAVS GQRLSADCRL
PHEARIVDVA RWPALAAPWL DVATRRAARL PPLAADCVDD GRERALGLRI DGIVDGSRLA
APPGEPGHIG VSAPEARGQV QWLLDGRWVG SSRDGGEFRL PLDMPAGRHS LTAMAENGAW
ARLEFERIVV AAR
//
