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Database: UniProt
Entry: A0A0K1FBC7_9MICO
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Original site: A0A0K1FBC7_9MICO 
ID   A0A0K1FBC7_9MICO        Unreviewed;       891 AA.
AC   A0A0K1FBC7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Multidrug ABC transporter permease {ECO:0000313|EMBL:AKT52019.1};
GN   ORFNames=ADJ73_13360 {ECO:0000313|EMBL:AKT52019.1};
OS   Arsenicicoccus sp. oral taxon 190.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Arsenicicoccus.
OX   NCBI_TaxID=1658671 {ECO:0000313|EMBL:AKT52019.1, ECO:0000313|Proteomes:UP000065578};
RN   [1] {ECO:0000313|Proteomes:UP000065578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0371 {ECO:0000313|Proteomes:UP000065578};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP012070; AKT52019.1; -; Genomic_DNA.
DR   RefSeq; WP_050348662.1; NZ_CP012070.1.
DR   AlphaFoldDB; A0A0K1FBC7; -.
DR   STRING; 1658671.ADJ73_13360; -.
DR   KEGG; ars:ADJ73_13360; -.
DR   PATRIC; fig|1658671.3.peg.2721; -.
DR   OrthoDB; 190266at2; -.
DR   Proteomes; UP000065578; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          33..185
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          674..723
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   891 AA;  94016 MW;  E1E458C087B23C25 CRC64;
     MSTHRGSHGP GRLGVSDPTS WEADVVLRDG SVCHLRPIRP SDRALIQAFH AKQSPESIYL
     RFFAPIKEIS AKDLTRFTEV DQVDRVALVA TVRDDIIGIG RYDVVDPGVA EVAFNISDHY
     QGKGIGSVLL EHLAAIGQEL GIEEFVADVL PQNRKMMKVF TDAGYEVKHH FDDGVIAVSF
     QIRPTVRSEM VRLSREHRSE AASIKTVLEP DSVVVVGASP RVEALGHLIL DNLVRGGFAG
     RTYAVHPTAT EVLGVPCRPT VSAIGEPIDL AVVAVPASEV LGVVDDCAAA GVKSLVVASN
     GFAESGPEGL RLQQELRARA HANGLRVVGP NTIGVANSTL HLNATVAPRL PHPGRLGLFA
     QSGALGVAVL ATAARRNVGV SVFASAGNRA DVSGNDLMQY FIDDPHTEAV GMHLESVGNP
     RKFSRIARQL AASKPVIVVK SGYSGYSVPP GHTVRPTQVP RAAFDAMMTQ AGVMRVENVH
     QLFDVAALVT SQPLPAGRRV GIVGNAHALG ALTADACLDR GLVVTHGPVS LAPEASAQEF
     AAALHAALDD EQVDAVVTCF IPPLVTADES VVSTVSEVAA QATKPILSTF LGMRGVADPS
     AGPTLGHGGV PTYPMPEDAV LALDKVSRYA AWRDTDKGER VTYEDIDRHA AFAVIDQVLQ
     DAPAGRALTD DEAGLLLRAY GVPVWPRVRV ASADEAVAAA ERLGHPVMMK SVSQVLRHSP
     GLGALRLDLD DAEEVREAFA HLTARFGSLG DPALVVQAMA SPGVACVIRS TEDTLFGPVV
     SFSVAGPPTE LLEDVAHRIP PLTDHDVHEL VTSVKAFPLL DGHRGAEPVD LPALEEIIGR
     ISVLADDFPE VSALELNPVQ ASAGGVEVLG AEIAVAKPGL RTDADRRAMT A
//
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