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Database: UniProt
Entry: A0A087E855_9BIFI
LinkDB: A0A087E855_9BIFI
Original site: A0A087E855_9BIFI 
ID   A0A087E855_9BIFI        Unreviewed;       770 AA.
AC   A0A087E855;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=BISU_0432 {ECO:0000313|EMBL:KFJ03956.1};
OS   Bifidobacterium subtile.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=77635 {ECO:0000313|EMBL:KFJ03956.1, ECO:0000313|Proteomes:UP000029055};
RN   [1] {ECO:0000313|EMBL:KFJ03956.1, ECO:0000313|Proteomes:UP000029055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11597 {ECO:0000313|EMBL:KFJ03956.1,
RC   ECO:0000313|Proteomes:UP000029055};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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:KFJ03956.1}.
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DR   EMBL; JGZR01000006; KFJ03956.1; -; Genomic_DNA.
DR   RefSeq; WP_024463268.1; NZ_JGZR01000006.1.
DR   AlphaFoldDB; A0A087E855; -.
DR   STRING; 77635.BISU_0432; -.
DR   eggNOG; COG0744; Bacteria.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000029055; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; 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: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:SF34; 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   Glycosyltransferase {ECO:0000313|EMBL:KFJ03956.1};
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:UP000029055};
KW   Transferase {ECO:0000313|EMBL:KFJ03956.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        60..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          110..283
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          378..625
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..54
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..707
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  82671 MW;  BF557A132230D79A CRC64;
     MASQTRSVSS RTGGTRARGS AGSHGGASPD PRSHRSSKQS HRPKGRKPRK NKPRHRVHRV
     LLWLLGIAAA LLLVGAGVFA YLYVTTEIPP AEKVALSSKT TVYYADGSTE IGSFAEQNRE
     IISCNALPKY VGQAIVSSEN RSFYTDKGID LKGIGRAFLS NITTNSRQGG STITQQYVKQ
     YYMGETVTSS YSAKLRQAIL AVKITQTQSK DQVLCNYMNT IYLGRGAYGI EAAAKAYFNK
     DAKDLTVSEA AMLAGIIPSP SNWDPAENPK QAQIRFERVL KIMREDGYIN GQDASSAKFP
     QTAQNAQQNT YAGQQGYLLE MVREELTKDK TFTKEELDTG GYKIVTTIDK AKQDLMFQVA
     SPSQDGNGVV PQGLQTGAMS VNPKDGSIIS LYAGDDYLTK QLNNATQATY EPGSTMKPFA
     LLAAVQDGMN LNTTFNGNSP RSFDGIASPV QNFGNQSFGY INMYNATANS VNTVYMELQQ
     DLGAKKVAQT ANKAGVSANR VKGDNPFTVL GNDGVHVQDI TQAFATIANQ GSKPTLHIVS
     KVTDTKGKSM YEAPTKTQRV FAANDTALVT KAMTGTVQYG TATEALSVGR TMAGKSGTAN
     DATAGSFVGF TPDTVSVFAM WYPDQNGNPQ EIPPFGIYSG GSDYPVHMFT QYMKQALAGT
     ADQAFPTAND TGKVGGPDGT WGTGSRTWQQ QQDQAEAKRK ADEQAQQDAQ NDRGTPTQTP
     SSPQPTQTPE DTQSASPIPN VPAPSNSQDD TSKNSQQQGT GKSEQGKNNG
//
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