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Database: UniProt
Entry: R9C480_9BACI
LinkDB: R9C480_9BACI
Original site: R9C480_9BACI 
ID   R9C480_9BACI            Unreviewed;       687 AA.
AC   R9C480;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=A499_09304 {ECO:0000313|EMBL:EOR24097.1};
OS   Niallia nealsonii AAU1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1202533 {ECO:0000313|EMBL:EOR24097.1, ECO:0000313|Proteomes:UP000014030};
RN   [1] {ECO:0000313|EMBL:EOR24097.1, ECO:0000313|Proteomes:UP000014030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAU1 {ECO:0000313|EMBL:EOR24097.1,
RC   ECO:0000313|Proteomes:UP000014030};
RA   Joshi C.G., Duggirala S.M., Nathani N.M., Bhatt V.D., KaPatel J.A.,
RA   Parnerkar S.P.;
RT   "Whole genome shotgun sequencing of Bacillus nealsonii AAU1.";
RL   Submitted (MAR-2013) 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:EOR24097.1}.
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DR   EMBL; ASRU01000100; EOR24097.1; -; Genomic_DNA.
DR   RefSeq; WP_016202522.1; NZ_ASRU01000100.1.
DR   AlphaFoldDB; R9C480; -.
DR   PATRIC; fig|1202533.3.peg.1934; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000014030; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        17..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..235
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          327..603
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          658..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   687 AA;  76497 MW;  6296123D1CAC11F2 CRC64;
     MEVIVNKLKN SGKYLRLLVI LGLLFMITAS IIFIGVYVYA RTLGPPPLAV SQSTIYYSDN
     GSIIGESSNG QKRYWVSIDD ISPYLVDATV SIEDKNFYSH HGFDYKRIGG AILADIKAMA
     KVQGASTITQ QYARNLFLEH EKTWKRKIAE AFYTLRLEIF YTKDEILEGY INTIYYGHGA
     YGAEAASQYY FGKEASKLTL AEATMLAGIP KGPSIYSPFS SIENAKKRQS IILNSLIENG
     YITAEDKRIA LNEKLSLVGE FPNTSMETAP YFQDSVKNIL KNQLHLDEKT IQLGGLRVYT
     TLNTEQQKIA EETINHTINK DSNIQIGFVA MDPTTGYVKA LVGGRNYEES PFNRATQASR
     QPGSTIKPLL YYAALEHGFT PATMMSSEKT TFRFDDGRDP YTPHNFNNRY ADGNITMAQA
     LAVSDNVYAV KTHLFLGQDT LVKTGKRFGI TTDLQEVPSL ALGTSNVRVI EMANAYSMFA
     NGGNSVSPVF ITKIETNDGQ ILYEHKAKKE KVLDTDLTFV MNQMMTGMFD PNLSGYASVT
     GSTIANDITR IYAGKSGSTE SDSWMIGYTP QLVSAVWTGY DQGEPITLTA DKTYAKKVWA
     QFMEQSLNKE PIKGFTPTKG TVGVYIDPKS GKLASNACGT KRIMYFTKET VPTEYCADLP
     KDDSSEKPAN KEKTNEKVPW YKRILPW
//
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