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Database: UniProt
Entry: A0A396SEV1_9BACI
LinkDB: A0A396SEV1_9BACI
Original site: A0A396SEV1_9BACI 
ID   A0A396SEV1_9BACI        Unreviewed;       684 AA.
AC   A0A396SEV1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=D1B33_04135 {ECO:0000313|EMBL:RHW40046.1};
OS   Lysinibacillus yapensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=2304605 {ECO:0000313|EMBL:RHW40046.1, ECO:0000313|Proteomes:UP000265692};
RN   [1] {ECO:0000313|EMBL:RHW40046.1, ECO:0000313|Proteomes:UP000265692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLB-03 {ECO:0000313|EMBL:RHW40046.1,
RC   ECO:0000313|Proteomes:UP000265692};
RA   Yu L.;
RT   "Lysinibacillus sp. YLB-03 draft genome sequence.";
RL   Submitted (AUG-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   -!- 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:RHW40046.1}.
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DR   EMBL; QWEI01000001; RHW40046.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A396SEV1; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000265692; Unassembled WGS sequence.
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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265692}.
FT   DOMAIN          66..237
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          327..572
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   684 AA;  76506 MW;  5B0F9B11AB35290B CRC64;
     MKRQNFRKQR KRKKWLKYTA FTVVAAFSAI IVGLITLRVY AQVAGAPPLT VPKASVFLDN
     NGHRIGDYFA AERRYWVELD EISPYLIDAT IAVEDKDFYE HSGFDYSRIA SALLTDLKTQ
     SMAEGASTLT MQLARNLYLS HAKTWTRKIQ EAMYAYRLEV FYDKDEILEG YLNTVNYGHG
     MYGVEAASRY YFGKSAGDLT LAESALLAGI PKGPSIYSPI NDFEKSIGRQ QVILSLMDSQ
     QYISTEEKER ANSEEIVLKN EQWTATKSIA PYFLDVAWQE AAGLLEKENL NIREGGWTIK
     TTLNQAHQKA AEEAVADNMP KSDLQVGFVS MDVRTGYVTA LVGGRNYEDS SFNRVTQAVR
     QPGSAIKPLL YAAALENGFT PLTYMDVGET IFTYDNGRAT YKPKNVNGQF AEGEMSLAQA
     LAISDNIYAV KTLEKIGYKP YQDILERFDL NVAGADNPSA ALGTTENSLF DITSAYNTIA
     NEGKKTKPTT ILEIKNGNGE VVYEYKPPEE KQVISEEDAF LLTDMMTGIF DPVFSDYSPA
     TGVSLRPRMT HTYAAKSGTT DSDQWIVGYT PSVTAGVWNG YDQGKTLSVQ QDMAATKHVW
     IDFMETVNKG KANESFKAPE GVEGVLIDIE TGKLATDACP KQRMMYLKTE DVPTEKCSSD
     FFDKESWDNF LDLFPFETFK NFFN
//
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