RBSA_CLOP1
ID RBSA_CLOP1 Reviewed; 501 AA.
AC Q0TPX5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Ribose import ATP-binding protein RbsA {ECO:0000255|HAMAP-Rule:MF_01716};
DE EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN Name=rbsA {ECO:0000255|HAMAP-Rule:MF_01716}; OrderedLocusNames=CPF_1882;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
CC -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose
CC import. Responsible for energy coupling to the transport system.
CC {ECO:0000255|HAMAP-Rule:MF_01716}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:29903, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:47013, ChEBI:CHEBI:456216; EC=7.5.2.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01716};
CC -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), two
CC transmembrane proteins (RbsC) and a solute-binding protein (RbsB).
CC {ECO:0000255|HAMAP-Rule:MF_01716}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01716};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01716}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Ribose importer
CC (TC 3.A.1.2.1) family. {ECO:0000255|HAMAP-Rule:MF_01716}.
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DR EMBL; CP000246; ABG84846.1; -; Genomic_DNA.
DR RefSeq; WP_003456071.1; NC_008261.1.
DR AlphaFoldDB; Q0TPX5; -.
DR SMR; Q0TPX5; -.
DR STRING; 195103.CPF_1882; -.
DR EnsemblBacteria; ABG84846; ABG84846; CPF_1882.
DR GeneID; 29571017; -.
DR KEGG; cpf:CPF_1882; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_2_9; -.
DR OMA; AKREIYQ; -.
DR OrthoDB; 551294at2; -.
DR Proteomes; UP000001823; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015611; F:ABC-type D-ribose transporter activity; IEA:RHEA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS51254; RBSA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Repeat;
KW Sugar transport; Translocase; Transport.
FT CHAIN 1..501
FT /note="Ribose import ATP-binding protein RbsA"
FT /id="PRO_0000261057"
FT DOMAIN 8..245
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT DOMAIN 255..500
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ SEQUENCE 501 AA; 55514 MW; 0A3D4ACC4F4292AE CRC64;
MGERTPMLKM VGVSKSFPGV KALDNVSLMA YGGEVTALMG ENGAGKSTLM KILSGVYKKD
EGKIFIEGRE VEVKGIKSAE EAGITIIHQE LSVLNNLTVS ENIFLGNEKH SKFTGRINKK
LLDERSKMFL EQIGCDIDPN RLVSTLNVGE KQMIEIAKAL TKNARIIIMD EPTTALTDVE
TENLFKVIEN LRKKGIAIIY ISHRMEEIFK ICHRVEVLRD GKYAGSAEIK DIDNDKLIAM
MVGRTIEDQF PYRDVKKGDL ALEVKNLSCK EGVKGASFTL RKGEILGIAG LMGSGRTELA
KTIFGEYKKT SGEISLNGSP ININCISDAI NNGICYLSED RKKEGCILGM SVGENMTLCN
LKKYENKFKS LDKKEEAKDI EYYIKKINIK TPNKEQFIKN LSGGNQQKVI LAKWLMLSPE
VLIIDEPTRG IDVGAKKEIY ELLNELKASG KAIIMISSDL PEVLGISDRI MVMSEGRISG
ELNRDEANQE SIMKLAVGIN N