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Database: UniProt
Entry: A0A0G0HS68_9BACT
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Original site: A0A0G0HS68_9BACT 
ID   A0A0G0HS68_9BACT        Unreviewed;       345 AA.
AC   A0A0G0HS68;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Methicillin resistance protein {ECO:0000313|EMBL:KKQ06726.1};
GN   ORFNames=US16_C0010G0010 {ECO:0000313|EMBL:KKQ06726.1};
OS   Candidatus Moranbacteria bacterium GW2011_GWE2_36_40.
OC   Bacteria; Candidatus Moranbacteria.
OX   NCBI_TaxID=1618713 {ECO:0000313|EMBL:KKQ06726.1, ECO:0000313|Proteomes:UP000033827};
RN   [1] {ECO:0000313|EMBL:KKQ06726.1, ECO:0000313|Proteomes:UP000033827}
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:KKQ06726.1}.
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DR   EMBL; LBRX01000010; KKQ06726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0HS68; -.
DR   STRING; 1618713.US16_C0010G0010; -.
DR   Proteomes; UP000033827; 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   345 AA;  40134 MW;  CE5064FFF57405FB CRC64;
     MDKSQNKDNF EKEFLQSFQW KRFQESVGRR THFIENDAFL ASIVEHVLSI VGKYMYVPRG
     PILNFKFEIL NEIQNLNNKI KNGMRELVDL GRKENAGWVR IEPESNQLLE LIKENISEKI
     VKAPHDMQPK EIFVLDISKN EEQLLAQMKP KTRYNISLAK KKNVVIRNSS LVTNEKKKEY
     ADAFLRLTKE MASRQGIVAH SQEYYRKMIE ILPAEMLKIY VAQYDGNIIA ANLVLFYENT
     VTYLHGASSN ENRNVMAPFL LQWQTILDAK ENGCMRYDFG GVRITNNSQQ TTNNWEGITN
     FKIGFSPNTK PIEFPGSYDI IINPRKYAVY RGLQRAKAFA VKFRK
//
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