ID I0S5W7_STRAP Unreviewed; 504 AA.
AC I0S5W7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, 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 Name=feoB {ECO:0000313|EMBL:EID18770.1};
GN ORFNames=HMPREF1043_0693 {ECO:0000313|EMBL:EID18770.1};
OS Streptococcus anginosus subsp. whileyi CCUG 39159.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1095729 {ECO:0000313|EMBL:EID18770.1, ECO:0000313|Proteomes:UP000003245};
RN [1] {ECO:0000313|EMBL:EID18770.1, ECO:0000313|Proteomes:UP000003245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 39159 {ECO:0000313|EMBL:EID18770.1,
RC ECO:0000313|Proteomes:UP000003245};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JAN-2012) 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 membrane {ECO:0000256|RuleBase:RU362098};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362098}.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362098}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EID18770.1}.
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DR EMBL; AICP01000075; EID18770.1; -; Genomic_DNA.
DR AlphaFoldDB; I0S5W7; -.
DR PATRIC; fig|1095729.3.peg.2196; -.
DR Proteomes; UP000003245; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01879; FeoB; 1.
DR Gene3D; 1.10.287.1770; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003373; Fe2_transport_prot-B.
DR InterPro; IPR041069; FeoB_Cyto.
DR InterPro; IPR030389; G_FEOB_dom.
DR InterPro; IPR011642; Gate_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00437; feoB; 1.
DR PANTHER; PTHR43185:SF1; FE(2+) TRANSPORTER FEOB; 1.
DR PANTHER; PTHR43185; FERROUS IRON TRANSPORT PROTEIN B; 1.
DR Pfam; PF17910; FeoB_Cyto; 1.
DR Pfam; PF02421; FeoB_N; 1.
DR Pfam; PF07670; Gate; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51711; G_FEOB; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|PIRSR:PIRSR603373-1,
KW ECO:0000256|RuleBase:RU362098};
KW Ion transport {ECO:0000256|RuleBase:RU362098};
KW Iron {ECO:0000256|RuleBase:RU362098};
KW Iron transport {ECO:0000256|RuleBase:RU362098};
KW Magnesium {ECO:0000256|PIRSR:PIRSR603373-2};
KW Membrane {ECO:0000256|RuleBase:RU362098};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603373-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR603373-1};
KW Transmembrane {ECO:0000256|RuleBase:RU362098};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362098};
KW Transport {ECO:0000256|RuleBase:RU362098}.
FT TRANSMEM 281..299
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 344..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 388..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT DOMAIN 1..164
FT /note="FeoB-type G"
FT /evidence="ECO:0000259|PROSITE:PS51711"
FT BINDING 8..15
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-2"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-2"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-2"
FT BINDING 33..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 53..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 113..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
SQ SEQUENCE 504 AA; 56060 MW; 590C2975552F2D23 CRC64;
MKELALAGNP NSGKTSLFNI LTGSSQHVGN WPGVTVEKKS GLFRKNKDII IQDLPGIYSL
SPYTSEEVIS RNYLLSGNAD GILDVVDATN LERNLYLSLQ LIETGILVVL ALNMSDVVVV
EKQGKWIDTT KLSYQLGVPV VATSALKKTG IDQVMRQALR EIERTDETIY PIYDSHFEAA
LSEIIRILGN AVPQKQARFY AIKLFERDKE LSEQLVLSDF QKTEIEDAIR ITEEIYTEDA
ETIVVNARYE FIESAVKMAL QADVNQLSLS DKIDRIVTNR YLALPIFAVV MWLVYFLSIQ
TIGTMGTDWT NDILFGEWIP NGVKSLLEQL AVADWLQSLI IDRIIAGCGA VLGFVPQIFV
LFICLGILED IGYMSRIAFV MDRIFRRFGL SGKSFIPMLI STGCGVPGVM ASRTIENERD
RRITIMTTTF MPCSAKLPII SLIAGAFFPS NIWIAPSAYF VGMGAIVLSG IALKKTAILN
CPQKVRQKIL VKGFSSVLHR TKSF
//
