RGMG_HAHCH
ID RGMG_HAHCH Reviewed; 515 AA.
AC Q2SMT0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Putative ribose/galactose/methyl galactoside import ATP-binding protein {ECO:0000255|HAMAP-Rule:MF_01717};
DE EC=7.5.2.11 {ECO:0000255|HAMAP-Rule:MF_01717};
DE EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01717};
GN OrderedLocusNames=HCH_01167;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
CC -!- FUNCTION: Part of an ABC transporter complex involved in carbohydrate
CC import. Could be involved in ribose, galactose and/or methyl
CC galactoside import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01717}.
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_01717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:60156, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.5.2.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01717};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01717}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01717}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Carbohydrate
CC importer 2 (CUT2) (TC 3.A.1.2) family. {ECO:0000255|HAMAP-
CC Rule:MF_01717}.
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DR EMBL; CP000155; ABC28044.1; -; Genomic_DNA.
DR RefSeq; WP_011395119.1; NC_007645.1.
DR AlphaFoldDB; Q2SMT0; -.
DR SMR; Q2SMT0; -.
DR STRING; 349521.HCH_01167; -.
DR EnsemblBacteria; ABC28044; ABC28044; HCH_01167.
DR KEGG; hch:HCH_01167; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_3_6; -.
DR OMA; EGMAVIM; -.
DR OrthoDB; 551294at2; -.
DR Proteomes; UP000000238; 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; PS51260; MGLA; 1.
DR PROSITE; PS51254; RBSA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Sugar transport;
KW Translocase; Transport.
FT CHAIN 1..515
FT /note="Putative ribose/galactose/methyl galactoside import
FT ATP-binding protein"
FT /id="PRO_0000262981"
FT DOMAIN 26..262
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT DOMAIN 272..511
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
SQ SEQUENCE 515 AA; 56653 MW; 09AC2EBDBDEB1A23 CRC64;
MSSASVVEAV SVNSAIPQNR NYEYVLEVAN VRKEFPGVVA LDNVSLRIRP GTVHALMGEN
GAGKSTLMKI IAGIYQPDKG QVLLRGEPVR LEKPLDAQEA GIAMIHQELL LMNPMTVAEN
IWIRREPKGR FGLIDHDEMR RRTQELFDRL NINLDPEAEI SELSVASRQM VEIAKAVSFN
SDVLIMDEPT SAITETEVAH LFDIIRDLRA KGIGIVYITH KMNELFEIAD EFSVFRDGQY
IGTHLSSNVT RDDIIRMMVG REVSQMFPKE EVALGDVVLS VKNLSREGVF RNVSFDVRAG
EIVGFAGLVG SGRSNVAEAL FGVAPADGGA IQINGEFVQI KSPNEAIQHG MAFLTEDRKE
TGCFLPLTIQ ENIQSAVLHQ NFVKKGFVAE AELAKEAVEI CNKLRVKTPG MDEVIENLSG
GNQQKVLIGR WLLTHPKILI LDEPTRGIDV GAKAEIHSLI TQLAHKGVAV VMISSELPEI
LGMSDRVVVM HEGRVTGILD RAEADQVKIM DLAAQ
