FEOB_METJA
ID FEOB_METJA Reviewed; 668 AA.
AC Q57986;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Fe(2+) transporter FeoB {ECO:0000305};
DE AltName: Full=Ferrous iron transport protein B;
GN OrderedLocusNames=MJ0566;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2] {ECO:0007744|PDB:2WJG, ECO:0007744|PDB:2WJH, ECO:0007744|PDB:2WJI, ECO:0007744|PDB:2WJJ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-165 IN COMPLEX WITH AND WITHOUT
RP GUANINE NUCLEOTIDES, FUNCTION, SUBUNIT, DOMAIN, GDP-BINDING, AND
RP MUTAGENESIS OF LYS-41 AND TYR-61.
RX PubMed=19615379; DOI=10.1016/j.jmb.2009.07.020;
RA Koster S., Wehner M., Herrmann C., Kuhlbrandt W., Yildiz O.;
RT "Structure and function of the FeoB G-domain from Methanococcus
RT jannaschii.";
RL J. Mol. Biol. 392:405-419(2009).
CC -!- FUNCTION: Probable transporter of a GTP-driven Fe(2+) uptake system,
CC might be able to transport Fe(2+) into or out of the cell (Probable).
CC {ECO:0000305|PubMed:19615379}.
CC -!- SUBUNIT: The crystallized N-terminal domain is a homodimer.
CC {ECO:0000269|PubMed:19615379}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255, ECO:0000305}.
CC -!- DOMAIN: The G protein domain (about resides 1-184) binds GDP faster and
CC with higher affinity than GTP and releases GTP much faster than GDP.
CC Release of bound nucleotide causes a rearrangement of GTP-binding
CC domain G5, which may transmit information about the nucleotide-bound
CC state from the G-domain to the transmembrane region of FeoB and effect
CC Fe(2+) transport. {ECO:0000269|PubMed:19615379}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. FeoB GTPase (TC 9.A.8) family.
CC {ECO:0000255|PROSITE-ProRule:PRU01048}.
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DR EMBL; L77117; AAB98557.1; -; Genomic_DNA.
DR PIR; F64370; F64370.
DR RefSeq; WP_010870070.1; NC_000909.1.
DR PDB; 2WJG; X-ray; 2.20 A; A/B=1-184.
DR PDB; 2WJH; X-ray; 2.10 A; A/B=1-165.
DR PDB; 2WJI; X-ray; 1.90 A; A/B=1-165.
DR PDB; 2WJJ; X-ray; 2.40 A; A/B=1-167.
DR PDBsum; 2WJG; -.
DR PDBsum; 2WJH; -.
DR PDBsum; 2WJI; -.
DR PDBsum; 2WJJ; -.
DR AlphaFoldDB; Q57986; -.
DR SMR; Q57986; -.
DR STRING; 243232.MJ_0566; -.
DR TCDB; 9.A.8.1.9; the ferrous iron uptake (feob) family.
DR EnsemblBacteria; AAB98557; AAB98557; MJ_0566.
DR GeneID; 1451431; -.
DR KEGG; mja:MJ_0566; -.
DR eggNOG; arCOG00359; Archaea.
DR HOGENOM; CLU_013350_3_0_2; -.
DR InParanoid; Q57986; -.
DR OMA; MEMPDYE; -.
DR OrthoDB; 27688at2157; -.
DR PhylomeDB; Q57986; -.
DR EvolutionaryTrace; Q57986; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR CDD; cd01879; FeoB; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003373; Fe2_transport_prot-B.
DR InterPro; IPR011640; Fe2_transport_prot_B_C.
DR InterPro; IPR041069; FeoB_Cyto.
DR InterPro; IPR030389; G_FEOB_dom.
DR InterPro; IPR011642; Gate_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR Pfam; PF07664; FeoB_C; 1.
DR Pfam; PF17910; FeoB_Cyto; 1.
DR Pfam; PF02421; FeoB_N; 1.
DR Pfam; PF07670; Gate; 2.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00437; feoB; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51711; G_FEOB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; GTP-binding; Ion transport; Iron;
KW Iron transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..668
FT /note="Fe(2+) transporter FeoB"
FT /id="PRO_0000210848"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 3..165
FT /note="FeoB-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048,
FT ECO:0000269|PubMed:19615379"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19615379,
FT ECO:0007744|PDB:2WJH"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19615379,
FT ECO:0007744|PDB:2WJH"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19615379,
FT ECO:0007744|PDB:2WJH"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19615379,
FT ECO:0007744|PDB:2WJH"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19615379,
FT ECO:0007744|PDB:2WJH"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19615379,
FT ECO:0007744|PDB:2WJH"
FT BINDING 35..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048,
FT ECO:0000269|PubMed:19615379"
FT BINDING 56..59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048,
FT ECO:0000269|PubMed:19615379"
FT BINDING 145..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048,
FT ECO:0000269|PubMed:19615379"
FT MUTAGEN 41
FT /note="K->A: Slight decrease in GTP hydrolysis rate."
FT /evidence="ECO:0000269|PubMed:19615379"
FT MUTAGEN 61
FT /note="Y->F: No change in GTP hydrolysis rate."
FT /evidence="ECO:0000269|PubMed:19615379"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2WJI"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:2WJI"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2WJH"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2WJI"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:2WJI"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2WJI"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:2WJI"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:2WJI"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2WJG"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:2WJI"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:2WJI"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:2WJI"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:2WJI"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2WJI"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2WJI"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:2WJI"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:2WJJ"
SQ SEQUENCE 668 AA; 74455 MW; 2145495E1150C19E CRC64;
MKSYEIALIG NPNVGKSTIF NALTGENVYI GNWPGVTVEK KEGEFEYNGE KFKVVDLPGV
YSLTANSIDE IIARDYIINE KPDLVVNIVD ATALERNLYL TLQLMEMGAN LLLALNKMDL
AKSLGIEIDV DKLEKILGVK VVPLSAAKKM GIEDLKKAIS IAVKDKKTAE IKYPNFEPYI
KKITSILQKD EDLKKYNLRY LAIKLLENDK YVEEIVKNSK VWNELKPVLD SIINELSKKY
GEAELGIVEE RYKVIDKIVK EVMKKTSGKL TTTEMLDDVL TDEKIGTLLI IPFLWMLFKF
TFDVSKPFSA MIEYFFGFLS EVVKSSISNK FIASLLADGI ISGVGAVLVF FPILAFLFFA
ISFLEDSGYM ARIPFITDRI MNKFGLPGKA VISMVMGFGC NVPAIMATRT IEDEKDRILT
ILINPLLSCS ARLPIYALFA GALFSKYQGV VILSMYALGV VLALITAFLF RKLIFKTSPS
YLIVELPPYH IPHLNVVLKN TWERVYDFLR KAGTIIVFGV ILVWVLSVYG PSGYLGEEVF
ENPQLIANSW VAVIGKTLAP LFSPMGWDWR ACSALVFGII AKEVVVGSLA MLYGTGEENL
SSVIAHAFSP VSAYAFMAFS LIYLPCIATL AVIKQEIGWK WALFAVTYEM ILAYVVALVI
SVIGNLLF
