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Database: UniProt
Entry: A0A0G1SGS9_9BACT
LinkDB: A0A0G1SGS9_9BACT
Original site: A0A0G1SGS9_9BACT 
ID   A0A0G1SGS9_9BACT        Unreviewed;       330 AA.
AC   A0A0G1SGS9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Methicillin resistance protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UX45_C0015G0017 {ECO:0000313|EMBL:KKU32555.1};
OS   Candidatus Uhrbacteria bacterium GW2011_GWF2_46_218.
OC   Bacteria; Candidatus Uhrbacteria.
OX   NCBI_TaxID=1619001 {ECO:0000313|EMBL:KKU32555.1, ECO:0000313|Proteomes:UP000034705};
RN   [1] {ECO:0000313|EMBL:KKU32555.1, ECO:0000313|Proteomes:UP000034705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the FemABX family.
CC       {ECO:0000256|ARBA:ARBA00009943}.
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:KKU32555.1}.
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DR   EMBL; LCMG01000015; KKU32555.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1SGS9; -.
DR   PATRIC; fig|1619001.3.peg.709; -.
DR   Proteomes; UP000034705; Unassembled WGS sequence.
DR   GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.30; -; 2.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR003447; FEMABX.
DR   PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   PANTHER; PTHR36174:SF1; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   Pfam; PF02388; FemAB; 2.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR   PROSITE; PS51191; FEMABX; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
SQ   SEQUENCE   330 AA;  38342 MW;  2EE5870E8855D308 CRC64;
     MEWLPWEHAQ LWNAFLIQNG PRSGAFLQSW EWGKYREALG DRIVRYAFVK EGEIKGVAML
     VEIERPLGIH FVYCPRGPVF SSDISTVERL AATRLLGSLC HMDFLRFEPA WEGERLKKEH
     QSPAIQPPDT LILDLTQFEE TLLSAMHHKT RYNIRLAERK GVLIERKKSE EWKDVWSLFE
     ETAKRDGFRL HPCEHYQKLL ECVNGSLGGA CTHLVTASFE GTSIAAALFV DIAGTRTYLH
     GATSNLYREV MAPYLLHWQE IMEAKKSAMG WYDFWGISHT HPSWAGFTRF KKGFGGEEVH
     YPGTYDFIMD YPKYFLYAVS RRLIYGRRHR
//
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