ID A0RDF0_BACAH Unreviewed; 636 AA.
AC A0RDF0;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:ABK85243.1};
GN OrderedLocusNames=BALH_1927 {ECO:0000313|EMBL:ABK85243.1};
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK85243.1, ECO:0000313|Proteomes:UP000000761};
RN [1] {ECO:0000313|EMBL:ABK85243.1, ECO:0000313|Proteomes:UP000000761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam {ECO:0000313|EMBL:ABK85243.1,
RC ECO:0000313|Proteomes:UP000000761};
RX PubMed=17337577; DOI=10.1128/JB.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
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DR EMBL; CP000485; ABK85243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RDF0; -.
DR KEGG; btl:BALH_1927; -.
DR HOGENOM; CLU_000604_36_0_9; -.
DR Proteomes; UP000000761; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR CDD; cd03221; ABCF_EF-3; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032524; ABC_tran_C.
DR InterPro; IPR032781; ABC_tran_Xtn.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR PANTHER; PTHR42855; ABC TRANSPORTER ATP-BINDING SUBUNIT; 1.
DR PANTHER; PTHR42855:SF1; ABC TRANSPORTER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF16326; ABC_tran_CTD; 1.
DR Pfam; PF12848; ABC_tran_Xtn; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ABK85243.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 9..260
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 324..543
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 605..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 72169 MW; 1FAE349C4DC15EEC CRC64;
MECTNMKMLT VENLSKSYGE KPLFDGLSFS IAEGQRAGII GVNGTGKSTL LKIIAGAEIP
DTGDMTHSRG YTISYLSQQP EFDEQLTVLE QVFHGDTPLI RLLRDYEKAL LHIEKDPSNE
KVQEQLFAVQ QRMDAMGAWE ANANAKSLLT KLGITDFTAT VGNLSGGQKK RIAMAQCFIE
TPDLLILDEP TNHLDHETVE WLEEYLARYT GAVLLVTHDR YFLDRVTNRI FELDNGKLYS
YEGNYSTFLE AKALREEQEL AQESKRQNLY RRELAWIRRG AKARSTKQKA RIQRFEELKG
QEGPAAKQSV DIALSGSRLG KKVLELKDVT KKFGNKTVLN NFNHIVKPGD RIGIIGANGS
GKSSLLNMLA GKISPDSGEI EVGQTVKIAY YTQENEEMNL NQRMIEYIKE IAEVIHTTDG
KVIGASQMLE RFLFPPHSHG TPLGKLSGGE RRRLYLLRIL MGEPNVLLLD EPTNDLDTQT
LTVLEDYLED FPGVVLTVSH DRYFLDKVVD ELFIFTGEGE VREFLGSYTD YLEMEKTREL
IEKAEVQKEK KVVEEAPKQQ RKRKLSYNEQ REWETIEDTI AELEEKLESI GEELANVGSD
FTKAQELSEA QQKTEEELEK TMERWSELSD IVEGLK
//
