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Database: UniProt
Entry: A0A0G0HB32_9BACT
LinkDB: A0A0G0HB32_9BACT
Original site: A0A0G0HB32_9BACT 
ID   A0A0G0HB32_9BACT        Unreviewed;       202 AA.
AC   A0A0G0HB32;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Methicillin resistance protein {ECO:0000313|EMBL:KKQ40488.1};
DE   Flags: Fragment;
GN   ORFNames=US58_C0019G0001 {ECO:0000313|EMBL:KKQ40488.1};
OS   Candidatus Magasanikbacteria bacterium GW2011_GWA2_37_8.
OC   Bacteria; Candidatus Magasanikbacteria.
OX   NCBI_TaxID=1619036 {ECO:0000313|EMBL:KKQ40488.1, ECO:0000313|Proteomes:UP000034333};
RN   [1] {ECO:0000313|EMBL:KKQ40488.1, ECO:0000313|Proteomes:UP000034333}
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:KKQ40488.1}.
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DR   EMBL; LBTN01000019; KKQ40488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0HB32; -.
DR   STRING; 1619036.US58_C0019G0001; -.
DR   Proteomes; UP000034333; 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; -; 1.
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); 1.
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}.
FT   NON_TER         202
FT                   /evidence="ECO:0000313|EMBL:KKQ40488.1"
SQ   SEQUENCE   202 AA;  23666 MW;  E241CBEE9881D14D CRC64;
     MINYLQNKKC IFFRVEPNHL SIINDSKFLI HQSIDINPRT TAILNLQQTD EALLDAMRKN
     TRYSIRFAGK QNLVVKEEKN LAVFWDLLQQ TAKHDNFTTH VKKHYEAIFN FNSIYQLTAF
     KDDIAIATAV FVGFGNTFTY LFAASDYKRH QLLAPYLLQW EAIKLGQKLG YKYYDFFGIA
     PRMKGVKSKE KGISEHEYDE RH
//
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