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Database: UniProt
Entry: A0A0G1MTS7_9BACT
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Original site: A0A0G1MTS7_9BACT 
ID   A0A0G1MTS7_9BACT        Unreviewed;       325 AA.
AC   A0A0G1MTS7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=FemAB family protein {ECO:0000313|EMBL:KKU11614.1};
GN   ORFNames=UX16_C0010G0005 {ECO:0000313|EMBL:KKU11614.1};
OS   Parcubacteria group bacterium GW2011_GWB1_45_7.
OC   Bacteria.
OX   NCBI_TaxID=1618878 {ECO:0000313|EMBL:KKU11614.1, ECO:0000313|Proteomes:UP000034347};
RN   [1] {ECO:0000313|EMBL:KKU11614.1, ECO:0000313|Proteomes:UP000034347}
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:KKU11614.1}.
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DR   EMBL; LCLD01000010; KKU11614.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1MTS7; -.
DR   Proteomes; UP000034347; 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   325 AA;  37751 MW;  1415580ADB390FDE CRC64;
     MIHLVEPKDK KEWDELLLGH NGSFTQSWQW GEMQKREGGK ALRFSILRDN NVLGCLSLYV
     RKTPAGFYGY IPRGPAVGER DLSDKDWSDL LELLHEIAKR EDLVFLLFEP VYPGAFGNLR
     AAENRQPNKT IFIDLLNPLE DLLSRINKTK RYGIRYAENH GVTVRISDKS KTDFEKFWKL
     LQGTAARKQF GTFSRSHFEN IFYEDISKMF LAEYEGHVEA AAEVIFFGDT AIYLHAGTSG
     KNEKLMASYL LVWEILKKAK QDGLKYLDLW GIDHNRWPGV TAFKESFGGR EITYPDARLV
     VYKRFRYFVY KLMHAVRNLL QRFTG
//
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