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Database: UniProt
Entry: H4GKW8_9LACO
LinkDB: H4GKW8_9LACO
Original site: H4GKW8_9LACO 
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}.
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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
//
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