ID A0A0J6ND82_9NEIS Unreviewed; 724 AA.
AC A0A0J6ND82;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=VK98_17200 {ECO:0000313|EMBL:KMN78026.1};
OS Chromobacterium sp. LK11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=1628212 {ECO:0000313|EMBL:KMN78026.1, ECO:0000313|Proteomes:UP000036114};
RN [1] {ECO:0000313|EMBL:KMN78026.1, ECO:0000313|Proteomes:UP000036114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LK11 {ECO:0000313|EMBL:KMN78026.1,
RC ECO:0000313|Proteomes:UP000036114};
RA Chan X.Y.;
RT "Draft genome of Chromobacterium aquaticum LK11.";
RL Submitted (MAY-2015) 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:KMN78026.1}.
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DR EMBL; LDUR01000029; KMN78026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6ND82; -.
DR STRING; 1628212.VK98_17200; -.
DR PATRIC; fig|1628212.3.peg.2587; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000036114; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; 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 Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00022519};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000036114};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..724
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005278694"
FT DOMAIN 44..221
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 302..545
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 624..703
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 724 AA; 78184 MW; A449F32425F54D09 CRC64;
MKGWTWLAAL ALCGAAAQAQ AQPSFQQVKA EWRPSDVVVL DRNGQPLQRL RVDKQGRRLD
WVSLADTSPA FRHALVVSED RRFYQHSGVD WSGVAAAAWG NLWNTRTRGA STLTMQLAGL
LDNDLKIGRN GRSLWQKMGQ GWSAAWLETH WSKAQILEAY LNLVGFRGEL VGLSALSATL
FGKLPAGLNL EESAIAVALI RAPNAAPDKV AARACRILQD MRRQPNCAAL AVRARQALAQ
SRAANPLAEQ DAPHFAQKLL QRQPLAAGSR VGSTLDLGLQ RYAVSVLRRH LAALAQRNVQ
DGALVVLDNA SGDILAWVGS SGRGLSNAAE VDGVTSLRQA GSTLKPFLYQ LALERRYLSA
ASLLNDSPLD LQTGSGLYAP QNYAKDFKGL VSARTALASS LNVPAVRAIE MVGPNALRDR
LYRLGLSSLQ QDGDYYGYSL ALGAADIRLL ELANAYRTLA NQGLASPARW TLADPKPKPQ
RQLDAASSFI IADILSDRTA RARTFGLESA LSTRYWSAVK TGTSKDMRDN WAVGFSRQRT
VAVWVGNAAG EPMWDVSGMH GAAPVWQAVL DRAQQGAPAS LPPAPPPGVV SQNVRYEGDV
EASRREWFLA GTERALIVPE RGGTSQTPGI AAPVDGSVYA LDPDIPPANQ RLLLRARGVA
RPQWWLNGKR LGSGASLPWF PWPGRHALEL RDAKGLVVEK IRFEVRGAVA VPGRKAGKAG
SRVN
//
