GenomeNet

Database: UniProt
Entry: W9ELT4_9LACO
LinkDB: W9ELT4_9LACO
Original site: W9ELT4_9LACO 
ID   W9ELT4_9LACO            Unreviewed;       777 AA.
AC   W9ELT4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=B808_443 {ECO:0000313|EMBL:ETO40644.1};
OS   Fructilactobacillus florum 8D.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Fructilactobacillus.
OX   NCBI_TaxID=1221538 {ECO:0000313|EMBL:ETO40644.1, ECO:0000313|Proteomes:UP000019474};
RN   [1] {ECO:0000313|EMBL:ETO40644.1, ECO:0000313|Proteomes:UP000019474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8D {ECO:0000313|EMBL:ETO40644.1,
RC   ECO:0000313|Proteomes:UP000019474};
RA   Kim E.B., Marco M.L.;
RT   "Genome sequencing of Lactobacillus florum 8D.";
RL   Submitted (AUG-2012) 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   -!- 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:ETO40644.1}.
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; ALXG01000017; ETO40644.1; -; Genomic_DNA.
DR   RefSeq; WP_035421645.1; NZ_ALXG01000017.1.
DR   AlphaFoldDB; W9ELT4; -.
DR   PATRIC; fig|1221538.3.peg.447; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000019474; 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   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:UP000019474};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..248
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          345..593
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          668..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  86913 MW;  864F008308B5CDC4 CRC64;
     MSSDETYSRL QKNKRKARPF LHIFLWIVFF VFLLFLMGVG LFTYYAASAP HVSYHTLSSD
     NSTTIYDRNG QVISRLGMQN RDYVKHQDIP ENLKNAIISV EDRHFYQDKG VDPIRIVEAG
     VSNIFGRSGG LQGGSTLTQQ LIKLSVFSTK ASDQTLKRKA QEAWLAVKVD KDYSKQQILE
     FYINKVYMGN NSYGMQTISQ TLYHKPLNQL DLAQTALLAG LPQAPVAYNP VTNPKYATIR
     RNQVLDAMVK NKAISQKQAN QAKRQNVQNG IDKANVNKTP TQKDEKYADA YISQVTQEMR
     AKGFNLNAGN KIYTNLDMNT QKHMYQLAND DNAGLAFNNN DFQIGATMVN PQNGKVVSML
     GSRKQNVLFG LNRAVQTDHS SGSTMKPLMD YGPAIEYLKY PTYQSMKDTP FTYPGTDKQL
     NDFDNKHQGT ITMRQALVQS RNIPAIRTLQ DVGIPRATEF LKGLGMTFKE PLNLQNGIGA
     YISSEQEAAA YAAFANGGTY HEPYLINKIV TPTGESKQFK AKSHRAMSPA TAFMITDMLK
     GVMTDPQGSG TAANIAGLYQ AGKTGTTQYP DNYLNQVPKN ASMDSWFTGY TKNLSLSIWT
     GFDRPLEPDH YLSEPQTKIA QQFYKQVMER ASENQPNENW TKPDDVVKTK KNGQTQYYIV
     GHGADQTQRV NTTASQSQQA ADNQSVVPNQ ADNKQQDQTT NEPTNGMATP TEQTPTPINN
     DQPQNTPTPS ENQPSQPTQN NNQQPQTNQQ PDQQNQPSQP AQPQTDSNQQ QQQQPNQ
//
DBGET integrated database retrieval system