ID H4GKW8_9LACO Unreviewed; 723 AA.
AC H4GKW8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=PS3_11351 {ECO:0000313|EMBL:EHS85038.1};
OS Limosilactobacillus gastricus PS3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1144300 {ECO:0000313|EMBL:EHS85038.1, ECO:0000313|Proteomes:UP000004567};
RN [1] {ECO:0000313|EMBL:EHS85038.1, ECO:0000313|Proteomes:UP000004567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS3 {ECO:0000313|EMBL:EHS85038.1,
RC ECO:0000313|Proteomes:UP000004567};
RX PubMed=23846278;
RA Martin V., Cardenas N., Jimenez E., Maldonado A., Rodriguez J.M.,
RA Fernandez L.;
RT "Genome Sequence of Lactobacillus gastricus PS3, a Strain Isolated from
RT Human Milk.";
RL Genome Announc. 1:E00489-E00413(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 -!- 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:EHS85038.1}.
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; AICN01000072; EHS85038.1; -; Genomic_DNA.
DR AlphaFoldDB; H4GKW8; -.
DR STRING; 1144300.PS3_11351; -.
DR PATRIC; fig|1144300.3.peg.1704; -.
DR Proteomes; UP000004567; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A; 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 4: Predicted;
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:UP000004567};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..243
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 339..615
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 261..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 78065 MW; 76B5FBA48CF017CA CRC64;
MGYFLVDHKA LWKRIFLWLV GIFVLLVIAG AALFFYYASS APTITKSDLQ SQTGTTIYDA
NGKVVSRLGA QKRQYASSSE LPKTLKNAVV AVEDKNFYHE KLGISPTRIV KAAFSNVFHG
TSDGIQGGST ITQQLIKLSV FSTAKSDQTF KRKAQEAWLA YNITKKFSKD QILTYYLNKV
YMGNGVYGMK TAAQYYYGKD LDELSLAQTA MLAGIPQSPS VYNPLANTTY AKERRDVVLD
AMQTNGYITA SQAAAAKKES VTKGLDSSHG NVESSSSQVD EPVVDAYVKQ VIEELEDKGY
NPTTDSLKVH TSLDTDAQQE LYDDANENVS FPSDNVQVGV AVVDPHNGQV IAMLGGRKLD
SNTVYGYNRA VQQTRSSGST AKPLMDYGPA IEYLHWPTFH VLSDTAMTWP DATGTIKDFD
NKYQGNITMR QALVQSRNVP AIRALQAVGI SKATKFLKGL GISQKKAYTY SSGIALYISP
LQEAAAYAAF ANGGTYYEPY YVTSVTTQEG TTTNFKKQGS RAMTKGTAFM ITNMLEGVFT
GNGSGTSAYL SGVNQAGKTG TTNASDNNNN SGILDSWMTG YTKNYSISVW TGYDDNKNTL
TDSGAYSAQY LYKALMSYLD GENHASNWTM PSSLESVSVQ GVTQYMFKAY PFSIEYASGS
STSSTSSSSS TSSSSSSSDS SSASSESTSS ASSSMLSESV QTITQNSQST TDANTNNAAS
SGQ
//