FEOB_SALCH
ID FEOB_SALCH Reviewed; 772 AA.
AC Q57IW8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Fe(2+) transporter FeoB {ECO:0000305};
DE AltName: Full=Ferrous iron transport protein B;
GN Name=feoB; OrderedLocusNames=SCH_3438;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
CC -!- FUNCTION: Probable transporter of a GTP-driven Fe(2+) uptake system.
CC {ECO:0000250|UniProtKB:P33650}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P33650}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P33650}.
CC -!- INDUCTION: Iron uptake is repressed by the global regulator Fur.
CC {ECO:0000250|UniProtKB:P33650}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017220; AAX67344.1; -; Genomic_DNA.
DR RefSeq; WP_000736983.1; NC_006905.1.
DR AlphaFoldDB; Q57IW8; -.
DR SMR; Q57IW8; -.
DR EnsemblBacteria; AAX67344; AAX67344; SCH_3438.
DR KEGG; sec:SCH_3438; -.
DR HOGENOM; CLU_013350_3_0_6; -.
DR OMA; PLGYDWK; -.
DR Proteomes; UP000000538; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP 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; 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 SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00437; feoB; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51711; G_FEOB; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; GTP-binding; Ion transport; Iron;
KW Iron transport; Membrane; Nucleotide-binding; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..772
FT /note="Fe(2+) transporter FeoB"
FT /id="PRO_0000210824"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 3..169
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 BINDING 35..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
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 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT BINDING 149..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
SQ SEQUENCE 772 AA; 84142 MW; 5EA17A2C163BC61B CRC64;
MKKLTIGLIG NPNSGKTTLF NQLTGARQRV GNWAGVTVER KEGQFATTDH QVTLVDLPGT
YSLTTISSQT SLDEQIACHY ILSGDADLLI NVVDASNLER NLYLTLQLLE LGIPCIVALN
MLDIAEKQQV RIDVDALSTR LGCPVVPLVS TRGRGIEALK LAIDRHNAND NVELVHYAQP
LLREAGFLAD AMAQEMPLQQ RRWLGLQMLE GDIYSRAYAG EAAQNLDTSL ARLKDEMDDP
ALHIADARYQ CIAAICDVVS NTLTAEPSRF TRAVDKIILN RFLGLPIFLF VMYLMFLLAI
NIGGALQPLF DAGSVAIFIH GIQWIGYTLH FPDWLTIFLA QGLGGGINTV LPLVPQIGMM
YLFLSFLEDS GYMARAAFVM DRLMQALGLP GKSFVPLIVG FGCNVPSVMG ARTLDAPRER
LMTIMMAPFM SCGARLAIFA VFAAAFFGQN GALAVFSLYV LGIVMAVLTG LMLKHTIMRG
EASPFVMELP VYHVPHIKSL IIQTWQRLKG FVLRAGKVII IVSIFLSAFN SFSLSGKIVD
NINDSALASV SRVITPVFKP IGVHEDNWQA TVGLFTGAMA KEVVVGTLNT LYTAENIQDE
AFNPADFHLG DELLGAVDDT WQSLKDTFSL SVLANPIEAS KGDGEMATGA MGVMDQKFGS
AAAAYSYLIF VLLYVPCISV MGAIARESSR GWMGFSILWG LNIAYSLATL FYQVTSFSQH
PTYSLICILA VIVFNVVVLS LLRRARSRVD IELLATRKNV SSCCSGTAGN CH