ID W0ER94_9BACT Unreviewed; 801 AA.
AC W0ER94;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Ferrous iron transport protein B {ECO:0000256|ARBA:ARBA00031200, ECO:0000256|RuleBase:RU362098};
GN ORFNames=BARVI_00825 {ECO:0000313|EMBL:AHF11636.1};
OS Barnesiella viscericola DSM 18177.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC Barnesiella.
OX NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF11636.1, ECO:0000313|Proteomes:UP000018901};
RN [1] {ECO:0000313|EMBL:AHF11636.1, ECO:0000313|Proteomes:UP000018901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18177 {ECO:0000313|Proteomes:UP000018901};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; CP007034; AHF11636.1; -; Genomic_DNA.
DR RefSeq; WP_025277390.1; NZ_CP007034.1.
DR AlphaFoldDB; W0ER94; -.
DR STRING; 880074.BARVI_00825; -.
DR KEGG; bvs:BARVI_00825; -.
DR PATRIC; fig|880074.11.peg.174; -.
DR eggNOG; COG0370; Bacteria.
DR HOGENOM; CLU_013350_3_0_10; -.
DR OrthoDB; 9809127at2; -.
DR Proteomes; UP000018901; 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 3: Inferred from homology;
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 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 397..415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 452..478
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 535..561
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 625..646
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 740..762
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 774..796
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT DOMAIN 112..274
FT /note="FeoB-type G"
FT /evidence="ECO:0000259|PROSITE:PS51711"
FT BINDING 119..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 130
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 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-2"
FT BINDING 144..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 165..168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 225..228
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
SQ SEQUENCE 801 AA; 89398 MW; 1AF8B095CEAA1D71 CRC64;
MRLSDLKTGE KAVVVKVLGH GAFRKRIIEM GFVRGQTVLV ELNAPLKDPI KYKIMDYEIS
LRRSEASLVE VITPEEAEAV FADDHKGSSE SKLTPSEEDE CIQRALTKST KTINIALVGN
PNCGKTSLFN IASGAHEHVG NYSGVTVDAK QGFFEYNGYH FNIYDLPGTY SLSAYSPEEL
YVRRYLKDET PDVLVNVVVA SNLERNLYLT TELIDMDYRM VIALNMFDEL EQSGGKIDYQ
HLGNMIGVPI VPTVSRSGKG VNQLFDTIID VYEGRNEAVR HVHVNLGNVI ENGITPLKNM
LKQDPTCTRE FSPRYLAIKL LEGDAEVKKI LEGADSYPAL MKLRDQEVKE IETTLNEDIE
SAIANEKYGF ISGALAETYT PGDKEETKTT RLIDSFVTNK LFGFPIFIFL MWLMFEATFS
LGAYPMSWIE SFVAWLSDLV STYMPAGPLK DLLIDGVLGG VGGVIVFLPN ILILYLFISF
MEDSGYMARA AFIMDKIMHK IGLHGKSFIP LVMGFGCNVP AIMATRTIES RSSRLITILI
DPFISCSARI PIYILLVGTF FSQHASLVLV SLYLLGILVA IVTAKLLRRF LFKVDETPFV
MELPPYRMPT AKATLRHMWS KAEQYLRKMG GIILVASVII WALSYFPRPK EAYERELTPQ
EQMEQQSNSY LGRIGQAVTP LVEPLGFNWK VTTSLLSGTA AKELVVSTLG VLYSESDSDE
GVSLSQRISQ PNPETGKPDF TPLIALTFMV FVLLYFPCVA SVTAVIKESG SWKWGLFTIV
YNTCVAWIVA FLVYQIGSLF I
//