Y1680_STRA3
ID Y1680_STRA3 Reviewed; 558 AA.
AC Q8E3S6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Putative ABC transporter ATP-binding protein gbs1680;
DE EC=7.-.-.-;
GN OrderedLocusNames=gbs1680;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL766852; CAD47339.1; -; Genomic_DNA.
DR RefSeq; WP_000651256.1; NC_004368.1.
DR AlphaFoldDB; Q8E3S6; -.
DR SMR; Q8E3S6; -.
DR STRING; 211110.gbs1680; -.
DR EnsemblBacteria; CAD47339; CAD47339; CAD47339.
DR KEGG; san:gbs1680; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_86_7_9; -.
DR OMA; DPMTRLD; -.
DR Proteomes; UP000000823; 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..558
FT /note="Putative ABC transporter ATP-binding protein
FT gbs1680"
FT /id="PRO_0000092086"
FT DOMAIN 5..246
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 295..527
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 328..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 558 AA; 62662 MW; 73BB2D12CB40F631 CRC64;
MKDFIEWKDF TFQYDVQSEP TLKGINLSIP KGEKVLILGP SGSGKSTLGH CLNGIIPNTH
KGQYSGIFTI NHKNAFDLSI YDKSHLVSTV LQDPDGQFIG LTVAEDIAFA LENDVVAQEE
MTSIVEMWAK RLEIAPLLSK RPQDLSGGQK QRVSLAGVLV DDSPILLFDE PLANLDPQSG
QDIMALVDRI HQEQDATTII IEHRLEDVLY ERVDRVVLFS DGQIIYNGEP DQLLKTNFLS
EYGIREPLYI SALKNLGYDF EKQNTMTSID DFDFSELLIP KMRALDLDKH TDKLLSVQHL
SVSYDLENNT LDDVSFDLYK GQRLAIVGKN GAGKSTLAKA LCQFIPNNAT LIYNNEDVSQ
DSIKERAERI GYVLQNPNQM ISQAMVFDEV ALGLRLRGFS DNDIESRVYD ILKVCGLYQF
RNWPISALSF GQKKRVTIAS ILILNPEVII LDEPTAGQDM KHYTEMMSFL DKLSCDGHSI
VMITHDMQLM LEYTDRAIVI DNGLIAADDH PINILSNTEL LKKTHLKKTS LFALADRLGI
SPQKLTQWYI DNQGGKNG
