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
//