ID Q5LFM5_BACFN Unreviewed; 827 AA.
AC Q5LFM5;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Ferrous iron transport protein B {ECO:0000256|ARBA:ARBA00031200, ECO:0000256|RuleBase:RU362098};
GN ORFNames=BF9343_1287 {ECO:0000313|EMBL:CAH07068.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH07068.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH07068.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
RN [2] {ECO:0007829|PDB:7R7B}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-76.
RX PubMed=35271852; DOI=10.1016/j.jbc.2022.101808;
RA Sestok A.E., Brown J.B., Obi J.O., O'Sullivan S.M., Garcin E.D.,
RA Deredge D.J., Smith A.T.;
RT "A fusion of the Bacteroides fragilis ferrous iron import proteins reveals
RT a role for FeoA in stabilizing GTP-bound FeoB.";
RL J. Biol. Chem. 298:101808-101808(2022).
CC -!- FUNCTION: Probable transporter of a GTP-driven Fe(2+) uptake system.
CC {ECO:0000256|RuleBase:RU362098}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU362098}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU362098}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:0000256|RuleBase:RU362098}.
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DR EMBL; CR626927; CAH07068.1; -; Genomic_DNA.
DR RefSeq; WP_005795491.1; NZ_UFTH01000001.1.
DR PDB; 7R7B; X-ray; 1.50 A; A/B=1-76.
DR PaxDb; 272559-BF9343_1287; -.
DR GeneID; 66329735; -.
DR KEGG; bfs:BF9343_1287; -.
DR eggNOG; COG0370; Bacteria.
DR eggNOG; COG1918; Bacteria.
DR HOGENOM; CLU_013350_3_0_10; -.
DR BioCyc; BFRA272559:G1GHZ-1384-MONOMER; -.
DR Proteomes; UP000006731; Chromosome.
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:0046914; F:transition metal ion binding; IEA:InterPro.
DR CDD; cd01879; FeoB; 1.
DR Gene3D; 1.10.287.1770; -; 1.
DR Gene3D; 2.30.30.90; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR007167; Fe-transptr_FeoA.
DR InterPro; IPR003373; Fe2_transport_prot-B.
DR InterPro; IPR011640; Fe2_transport_prot_B_C.
DR InterPro; IPR038157; FeoA_core_dom.
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 InterPro; IPR008988; Transcriptional_repressor_C.
DR NCBIfam; TIGR00437; feoB; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43185:SF1; FE(2+) TRANSPORTER FEOB; 1.
DR PANTHER; PTHR43185; FERROUS IRON TRANSPORT PROTEIN B; 1.
DR Pfam; PF04023; FeoA; 1.
DR Pfam; PF07664; FeoB_C; 1.
DR Pfam; PF17910; FeoB_Cyto; 1.
DR Pfam; PF02421; FeoB_N; 1.
DR Pfam; PF07670; Gate; 2.
DR SMART; SM00899; FeoA; 1.
DR SUPFAM; SSF50037; C-terminal domain of transcriptional repressors; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51711; G_FEOB; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7R7B};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR603373-
KW 1}; Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362098};
KW Iron transport {ECO:0000256|ARBA:ARBA00022496,
KW ECO:0000256|RuleBase:RU362098};
KW Magnesium {ECO:0000256|PIRSR:PIRSR603373-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362098};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603373-2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR603373-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006731};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362098};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362098};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362098}.
FT TRANSMEM 444..465
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 500..524
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 544..566
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 578..604
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 668..689
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 769..791
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 800..822
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT BINDING 118..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-2"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-2"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-2"
FT BINDING 143..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 164..167
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 224..227
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
SQ SEQUENCE 827 AA; 93023 MW; B8617813E785626B CRC64;
MRLSELKTGE KGVIVKVLGH GGFRKRIVEM GFIKGKTVEV LLNAPLKDPI KYKIMGYEIS
LRRQEADMIE IISEQEAKSQ TQEAAYHQGL TEDIDVKEED LKRVALGKRR TINVALVGNP
NCGKTSLFNL ASGAHEHVGN YSGVTVDAKE GYFDFQGYHF KIVDLPGTYS LSAYTPEEIY
VRRHIIDETP DVIINVVDSS NLERNLYLTT QLIDMNVRMV VALNMYDELE ASGNTLDYLL
LGKLFGVPMV PTVCKRNIGV DRLFHVVINL YEGADFIDKK GHIHPEVAKE IMDWHQSLPN
FKDHGEHPAD YTHGKEPVGK VFRHIHINHG PDLEKAIDAV KEEISKNEFI RHKYSTRYLA
IKLLENDPEI ERFIHTLPNA VEVEKKRDKA ARRIQETMNE DSESALTDAK YGFISGALKE
TFTDNHLEQE QTTKVLDSIV THRIWGYPIF FLFMYLMFEG TFVIGEYPMM GIEWLVEALG
NLIRDNMSEG PLKDLMIDGI IGGVGGVIVF LPNILILYFC ISLMEDSGYM ARAAFIMDKI
MHKMGLHGKS FIPLIMGFGC NVPAIMASRT IENRKSRLIT MLVNPLMSCS ARLPIYLLLV
GAFFPKNGSL VLLAIYAIGI ALAVIMARLF SRFLVKGDDT PFVMELPPYR MPTMKSIFRH
TWEKGAQYLK KMGGIIMIAS IIIWFLGYYP DHDAYPTQAE QQENSYIGQI GQAVEPVLKP
LGFDWKLSIG LLSGVGAKEL VVSTLGVLYT NDADADVVSL AERIPITPLA AFSYMLFVLI
YFPCIATLVA IKQESGSWKW AIFTAGYTTA LAWLVSFAVY QIGGMFL
//