Y753_CLOTE
ID Y753_CLOTE Reviewed; 437 AA.
AC Q897I2;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Putative ABC transporter ATP-binding protein CTC_00753;
DE EC=7.-.-.-;
GN OrderedLocusNames=CTC_00753;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC -!- FUNCTION: Probably part of an ABC transporter complex. Responsible for
CC energy coupling to the transport system (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AE015927; AAO35354.1; -; Genomic_DNA.
DR RefSeq; WP_011099020.1; NC_004557.1.
DR AlphaFoldDB; Q897I2; -.
DR SMR; Q897I2; -.
DR STRING; 212717.CTC_00753; -.
DR EnsemblBacteria; AAO35354; AAO35354; CTC_00753.
DR KEGG; ctc:CTC_00753; -.
DR HOGENOM; CLU_000604_86_7_9; -.
DR OMA; YEACPND; -.
DR OrthoDB; 870493at2; -.
DR Proteomes; UP000001412; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transport.
FT CHAIN 1..437
FT /note="Putative ABC transporter ATP-binding protein
FT CTC_00753"
FT /id="PRO_0000092004"
FT DOMAIN 1..143
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 179..416
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 219..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 437 AA; 49703 MW; AA3B71413F017D2E CRC64;
MEREIAFGLE NFNTDINTMK RNVSEVISLL GLNKIRDKQT TEISGGEKQR VAIASVVSMD
PQIIAFDEPI SQLDPISAEE VLNSIKRLNR DLGKTIILVE QRLDKCFHMA DRIIFMENGE
IIGQGTPKNI PENIVNKYHL PTITYIFKEA GLQTLPITVK EGRDIIRNNK FQDLKEDDLK
FKEVVMEIEK LNFEYERGYK ILKDLSFKLH RGEIMTVMGE NGAGKSTLFK IIAGMIDKYK
GKVLIDNKNI KSLKLKERIK KIGYLSQNPN DYFGRKTVFE EVGYTLKNIG EYKEEKVEQV
MKLLNISYLE DKNPRDLSGG EKQRVAIACT IITDPEILIL DEPTRGMDAE AKENLGEIIK
TLAEVGKSIV VITHDSDFAG DYSHSVMLMF NGEIVAKGCA RDILYNSMYY SPQISKIFKN
KCNIISSKRA IELLKVI