FBPC2_RHIME
ID FBPC2_RHIME Reviewed; 395 AA.
AC Q92UV5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Fe(3+) ions import ATP-binding protein FbpC 2 {ECO:0000255|HAMAP-Rule:MF_01706};
DE EC=7.2.2.7 {ECO:0000255|HAMAP-Rule:MF_01706};
GN Name=fbpC2 {ECO:0000255|HAMAP-Rule:MF_01706}; OrderedLocusNames=RB0982;
GN ORFNames=SMb21541;
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; CAC49382.1; -; Genomic_DNA.
DR PIR; F95964; F95964.
DR RefSeq; NP_437522.1; NC_003078.1.
DR RefSeq; WP_010975826.1; NC_003078.1.
DR AlphaFoldDB; Q92UV5; -.
DR SMR; Q92UV5; -.
DR STRING; 266834.SM_b21541; -.
DR EnsemblBacteria; CAC49382; CAC49382; SM_b21541.
DR KEGG; sme:SM_b21541; -.
DR PATRIC; fig|266834.11.peg.5909; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_5; -.
DR OMA; RTAMPLM; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR017666; AminoethylPonate_ABC_PhnT2.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03265; PhnT2; 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..395
FT /note="Fe(3+) ions import ATP-binding protein FbpC 2"
FT /id="PRO_0000092363"
FT DOMAIN 23..264
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01706"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01706"
SQ SEQUENCE 395 AA; 43429 MW; 26FC92C3558E9A18 CRC64;
MHIAQELADE TCNSPRGAGH ARLRYPSDRR TAIPRNRRPL EGLWRFRRVR DIDLQVKEGE
FICFLGPSGC GKTTLLRAIA GLDIQSRGTI CQGGQDISRL PPAQRDYGIV FQSYALFPNL
TIEKNIAFGL ENIGRPRREI ASRVSELLEL VGLSSQGRKY PAQLSGGQQQ RVALARAMAI
SPGLLLLDEP LSALDAKVRV HLRHEIKELQ RKLGVTTIMV THDQEEALAM ADRIVVMNQG
GIEQVGTPTE IYRHPKTLFV ADFIGETNQF PATVGKGAQV EIGHTRFACA EHRLPSGASV
VAAVRPADII PHGAAAHRAT GLDAVGNADN LIDAHVEDME FLGMFWRTRL SAPRLKEKAL
VADFSTNAVR RLSIEIGSAI QVEIPQERLL LFAKA
