ID   Y1893_SACS2             Reviewed;         530 AA.
AC   Q97X60;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Putative ABC transporter ATP-binding protein SSO1893;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=SSO1893;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; AE006641; AAK42084.1; -; Genomic_DNA.
DR   PIR; E90353; E90353.
DR   RefSeq; WP_009992766.1; NC_002754.1.
DR   AlphaFoldDB; Q97X60; -.
DR   SMR; Q97X60; -.
DR   STRING; 273057.SSO1893; -.
DR   PRIDE; Q97X60; -.
DR   EnsemblBacteria; AAK42084; AAK42084; SSO1893.
DR   GeneID; 44130676; -.
DR   KEGG; sso:SSO1893; -.
DR   PATRIC; fig|273057.12.peg.1949; -.
DR   eggNOG; arCOG00188; Archaea.
DR   HOGENOM; CLU_000604_86_7_2; -.
DR   InParanoid; Q97X60; -.
DR   OMA; YEACPND; -.
DR   PhylomeDB; Q97X60; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   CDD; cd03225; ABC_cobalt_CbiO_domain1; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN           1..530
FT                   /note="Putative ABC transporter ATP-binding protein
FT                   SSO1893"
FT                   /id="PRO_0000092161"
FT   DOMAIN          6..243
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          282..516
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         314..321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   530 AA;  59832 MW;  CE7D001546B8C6D3 CRC64;
     MKFVEIRDLQ VTYMGKTKPS IVIDKLDIEE GESVLITGRS GSGKSTLVSV INGVIPHLIN
     AEVKGEVRVF GLDIKTTPTS EISRYVGTLL QDPDTQAFNY TVIDEVAFGV ENYMVSREEM
     INRVEESMKI CGISHLRDRE INTLSGGELQ RTVLASVLAM RPKALILDEP TSNIDPQGTR
     EILELVKTFR SEGISLVLVE HKIERVLPFI DRIIVVESGK IAVDIKKDEI IDRADLLHSL
     GLEIPDYMLF LKKSGFRRID YEYLRKTYNY KPPSRNEGKG EILFASVKVK TKSGKYLINT
     KISLKQGTIT ALMGKNGSGK TTLLKAIVGL IDKKRLIVEE EKVIVNGKDL SKAKLVERGK
     YLAYLPQFFD VMFIKRTVED EVKFSMKNRG VYDEMRLGEI LRIFSLDAYR TEDPLVLSMG
     QRRRVAMASV IAGGAKVILM DEPTSGQDWY HRQILGKELL ELRNKGYTIL VVTHDARFVD
     RFTDYLLVMS DGKIVLEGKP EEVFSKSLNH GIEPPLEYEL GGLIKNEQFS