Y430_STRR6
ID Y430_STRR6 Reviewed; 560 AA.
AC Q8DQY5;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putative ABC transporter ATP-binding protein spr0430;
DE EC=7.-.-.-;
GN OrderedLocusNames=spr0430;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(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; AE007317; AAK99234.1; -; Genomic_DNA.
DR PIR; F97925; F97925.
DR RefSeq; NP_358024.1; NC_003098.1.
DR RefSeq; WP_000656519.1; NC_003098.1.
DR AlphaFoldDB; Q8DQY5; -.
DR SMR; Q8DQY5; -.
DR STRING; 171101.spr0430; -.
DR EnsemblBacteria; AAK99234; AAK99234; spr0430.
DR GeneID; 60234492; -.
DR KEGG; spr:spr0430; -.
DR PATRIC; fig|171101.6.peg.473; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_86_7_9; -.
DR OMA; DPMTRLD; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; 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; 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;
KW Reference proteome; Repeat; Translocase; Transport.
FT CHAIN 1..560
FT /note="Putative ABC transporter ATP-binding protein
FT spr0430"
FT /id="PRO_0000092103"
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; 62761 MW; D672C970984A1265 CRC64;
MKEAIIEWKD FSFRYETQQE PTLQGIDLTI YKGEKVLIVG PSGSGKSTLG QCLNGIIPNI
YKGHTYGEFL IKGQAAFDMS IYDKSHLVST VLQDTDGQFI GLSVAEDLAF ALENDVTALD
EMKGRVYKWA EKLDLLPLLD QRPQDLSGGQ KQRVSLAGVL IDESPILLFD EPLANLDPKS
GQDIIELIDQ IHKEEGTTTL IIEHRLEDVL HCPVDRIVLI NDGRILFNGS PDQLLATDLL
TQNGIREPLY LTTLRQLGVD LVKEEQLADL DNLSISKGQV QLRTELVKET PELQSLFRLE
DVSFSYDDRP ILKSLHLDIK KGEKIAIVGK NGAGKSTLAK ALSSFIQTEG RYLWEGQDIK
GDSVAERAER VGYVLQNPNQ MISTNMIFDE VALGLRLRGV DEQEIETRVY ETLKICGLYE
FRNWPISALS FGQKKRVTIA SILVLGAEII LLDEPTAGQD QKNYTEIMEF LEELHQQGHT
IVMITHDMQL MLDYSDRALV MVDGELIADT DPASLLSNPE LLVKANLKET SIFNLAKKLD
VDPLALTAFY KERREGCKLN