FBPC1_RHIME
ID FBPC1_RHIME Reviewed; 353 AA.
AC Q92WJ0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Fe(3+) ions import ATP-binding protein FbpC 1 {ECO:0000255|HAMAP-Rule:MF_01706};
DE EC=7.2.2.7 {ECO:0000255|HAMAP-Rule:MF_01706};
GN Name=fbpC1 {ECO:0000255|HAMAP-Rule:MF_01706}; OrderedLocusNames=RB0349;
GN ORFNames=SMb20363;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Part of the ABC transporter complex FbpABC involved in Fe(3+)
CC ions import. Responsible for energy coupling to the transport system.
CC {ECO:0000255|HAMAP-Rule:MF_01706}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Fe(3+)(out) + H2O = ADP + Fe(3+)(in) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12332, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01706};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (FbpC),
CC two transmembrane proteins (FbpB) and a solute-binding protein (FbpA).
CC {ECO:0000255|HAMAP-Rule:MF_01706}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01706}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01706}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Fe(3+) ion
CC importer (TC 3.A.1.10) family. {ECO:0000255|HAMAP-Rule:MF_01706}.
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DR EMBL; AL591985; CAC48749.1; -; Genomic_DNA.
DR PIR; E95885; E95885.
DR RefSeq; NP_436889.1; NC_003078.1.
DR RefSeq; WP_010975241.1; NC_003078.1.
DR AlphaFoldDB; Q92WJ0; -.
DR SMR; Q92WJ0; -.
DR STRING; 266834.SM_b20363; -.
DR EnsemblBacteria; CAC48749; CAC48749; SM_b20363.
DR GeneID; 61600359; -.
DR KEGG; sme:SM_b20363; -.
DR PATRIC; fig|266834.11.peg.5278; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_5; -.
DR OMA; VYVSHDQ; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0015408; F:ABC-type ferric iron transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013611; Transp-assoc_OB_typ2.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08402; TOBE_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51242; FBPC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Ion transport; Iron;
KW Iron transport; Membrane; Nucleotide-binding; Plasmid; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..353
FT /note="Fe(3+) ions import ATP-binding protein FbpC 1"
FT /id="PRO_0000092362"
FT DOMAIN 9..239
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01706"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01706"
SQ SEQUENCE 353 AA; 37985 MW; 9D83D7E9ED7E9C5D CRC64;
MTVVAPGSVV FRNICKQFGA FTAIPDLSLT IEPGTLVTLL GPSGCGKTTT LRMLAGLEHP
TSGRILIGGK DVTMLPANER DVSMVFQSYA LFPHMNALDN VAYGLESSGM RRKEARERAE
EGLALVGLPG MGQRLPAELS GGQQQRVAVA RALVLEPQVL LLDEPLSNLD ARLRRRVRTE
IRELQQRLGF TAVYVTHDQD EALAVSDRII VMKDGNIAQE GPPRELYETP ASAFIADFMG
EANVVACDVI DVDGHEATIR VERLTHRVSG RGMRPGPAKL AVRPNAITLE PSAAGSFSGE
ITHTAYLGDH VEYEVKTAAG TLFVVDPAVE RALAPQTNVA IAFKERGIAL ING
