ID   Y483_STRPN              Reviewed;         560 AA.
AC   Q97SA3;
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 SP_0483;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=SP_0483;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(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; AE005672; AAK74642.1; -; Genomic_DNA.
DR   PIR; A95056; A95056.
DR   RefSeq; WP_000656548.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97SA3; -.
DR   SMR; Q97SA3; -.
DR   STRING; 170187.SP_0483; -.
DR   EnsemblBacteria; AAK74642; AAK74642; SP_0483.
DR   KEGG; spn:SP_0483; -.
DR   eggNOG; COG1122; Bacteria.
DR   OMA; DPMTRLD; -.
DR   PhylomeDB; Q97SA3; -.
DR   BioCyc; SPNE170187:G1FZB-501-MON; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR   CDD; cd03225; ABC_cobalt_CbiO_domain1; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR022216; ABC_Co_transporter.
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   Pfam; PF12558; DUF3744; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Repeat;
KW   Translocase; Transport.
FT   CHAIN           1..560
FT                   /note="Putative ABC transporter ATP-binding protein
FT                   SP_0483"
FT                   /id="PRO_0000092100"
FT   DOMAIN          6..247
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          297..528
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         329..336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   560 AA;  62873 MW;  4AD82F197FBED651 CRC64;
     MKEAIIEWKD FSFRYETQQE PTLQGIDLTI YKGEKVLIVG PSGSGKSTLG QCLNGIIPNI
     YKGQTYGEFL IKGQVAFDMS IYDKSHLVST VLQDTDGQFI GLSVAEDLAF ALENDVTALD
     EMKGRVYKWA EKLDLLPLLD QRPQDLSGGQ KQRVSLAGVL IDESPILLFD EPLANLDPKS
     GQDIIELIDQ IHKEEGTTTL IIEHRLEDVL HRPVDRIVLI NDGRILFNGS PDQLLATDLL
     TQNGIREPLY LTTLRQLGVD LVKEEQLANL DNLSISKGQV QLQNELAKET PALQSLFRLE
     EVSFSYDDRP ILKSLHLDIK KGEKIAIVGK NGAGKSTLAK AISSFIQTEG RYLWEKQDIK
     GDSVAERAER VGYVLQNPNQ MISTNMIFDE VALGLRLRGV DEKEIETRVY ETLKICGLYE
     FRNWPISALS FGQKKRVTIA SILVLGAEII LLDEPTAGQD QKNYTEIMEF LEELHQKGHT
     IVMITHDMQL MLDYSDRVLV MVDGELIADT VPASLLSDPE LLVKANLKET SIFNLAKKLD
     VDPLDLTAFY KERREGCKLN