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Database: UniProt
Entry: A0A498D6S2_9BACI
LinkDB: A0A498D6S2_9BACI
Original site: A0A498D6S2_9BACI 
ID   A0A498D6S2_9BACI        Unreviewed;       672 AA.
AC   A0A498D6S2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=D8M04_15000 {ECO:0000313|EMBL:RLL42854.1};
OS   Oceanobacillus piezotolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=2448030 {ECO:0000313|EMBL:RLL42854.1, ECO:0000313|Proteomes:UP000270219};
RN   [1] {ECO:0000313|EMBL:RLL42854.1, ECO:0000313|Proteomes:UP000270219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLB-02 {ECO:0000313|EMBL:RLL42854.1,
RC   ECO:0000313|Proteomes:UP000270219};
RA   Yu L.;
RT   "Oceanobacillus sp. YLB-02 draft genome.";
RL   Submitted (OCT-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:RLL42854.1}.
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DR   EMBL; RCHR01000005; RLL42854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498D6S2; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000270219; 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: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   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000270219};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          53..226
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          317..560
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   672 AA;  74871 MW;  235D74B10982798C CRC64;
     MKINLQLLSK LFIRIIGLIV LSFLSLSLIL FLLGPPSLTM DQNTIYYSSS GEVIGEEKGL
     GNRYWVELEH ISPSLVDATL AIEDRHFYKH HGFDFKRIAG AILKNIQSMS LEEGASTLTQ
     QLARNVYLSH EKTWSRKLKE AFYTVRIEMH YSKEEILEAY LNTIYFGHGA HGVEAASKHF
     FDKSAHELTL AESSMLAGIP KGPTYYSPFN HKVNAENRQQ LILQTMLDNG YISEEAYQDA
     KSHKLVYAPV DEKEQLEIGP YFQDEVLNEA ARLLKIDSES LRSGGYEIYT TMDIHMQKEL
     EQAIQHTVPT STELEVGAMA LDPLSGAVRA IVGGKSYAES PFNRAMDAKR MAGSTFKPFL
     YYAALANGYT PLTTLASTPT TFELEDGEVY QPSNFNNYYA YEPISLAQAI ALSDNIYAVK
     TNLFLTPERL VETASKFGIS EDLPAVPSLA LGTASVSVEE MVTAYGMLAN GGESVTGYLI
     EEIKDRNGKV VYKRDKPKKE LLLDPRYAFI LTDLLTGMFD RALDGYTSVT GSPIINQLTR
     TYAGKSGTTI SDSWMIGYSP SLVAGIWTGY DDNRPITLIK ENSYAKQIWA SFMESAHEGL
     PKQGFTAPPG VVAVPIDPVT GMRATGGCEE SRIMYFEEGT EPLEACSAHY DSYEKVEHRG
     FLEELFDSFL DR
//
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