ID A0A264Y8R0_9BACT Unreviewed; 841 AA.
AC A0A264Y8R0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Ferrous iron transport protein B {ECO:0000256|ARBA:ARBA00031200, ECO:0000256|RuleBase:RU362098};
GN Name=feoB {ECO:0000313|EMBL:OZT04484.1};
GN ORFNames=CHL74_04775 {ECO:0000313|EMBL:OZT04484.1};
OS Prevotella sp. 885.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2022527 {ECO:0000313|EMBL:OZT04484.1, ECO:0000313|Proteomes:UP000216632};
RN [1] {ECO:0000313|EMBL:OZT04484.1, ECO:0000313|Proteomes:UP000216632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=885 {ECO:0000313|EMBL:OZT04484.1,
RC ECO:0000313|Proteomes:UP000216632};
RA Efimov B.A., Chaplin A.V., Kochetkova T.O., Sokolova S.R., Ogneva L.V.,
RA Rebrikov D.V., Kondova I., Langermans J.A., Shkoporov A.N.;
RT "Description of Prevotella sp. 885 sp. nov., isolated from rhesus macaque
RT feces.";
RL Submitted (JUL-2017) 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}.
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:OZT04484.1}.
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DR EMBL; NOVE01000009; OZT04484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A264Y8R0; -.
DR OrthoDB; 9809127at2; -.
DR Proteomes; UP000216632; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000216632};
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 449..470
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 501..526
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 555..572
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 584..610
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 678..695
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 783..805
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 814..836
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 841 AA; 94546 MW; 9E0F5AE8D76F4420 CRC64;
MKLSDLKTGQ RGVIVKVTGH GGFRKRIVEM GFIKGKVVDV LQNAPLQDPV KYKIMGYEVS
LRHSEAEMIE VVSEEEAAKM ESRNETAEPI PASNHYLSDT QLRNAAMKKR RTINVALIGN
PNCGKTSLFN FASGAHERVG NYSGVTVDAK VGHASFEGYE FNIVDLPGTY SLSAYSPEEL
YVRKQIIEHT PDVIINVIDA SNLERNLYLT TQLIDMNLRM VCALNMFDET EKRGDNVDYT
RLGQLFGVPM IPTTFTTGRG VELLFHIIIN MYEGLDFLDT KGNMSPEIAE GIRQWHEQYD
KDKADSSDHE EDFASGIKPK NNVIRHIHIN HGQYVEAGIN SIQAILKEDG QLRHKYSTRY
LAIKLLEKDK EAVKLLDDGS EPSKKIFAAR DKAMADILEY THEDSETAIM DAKYGFIHGA
LKEAGYKTGD KKDTYFITHL IDNVITNKYV GFPIFLIMIW VMFEATFSLG QYPMEWIESL
VEWIGSLVSD NMPQGPIKDM LVDGVIGGVG SVIVFLPQIL ILYFFISFME DSGYMARAAF
IMDKLMHKMG LHGKSFIPLI MGFGCNVPAV MATRTIESKR SRFITMLILP LMSCSARFPI
YIMIIGTMFA QQYRSTIMFS LYIIGILMAV LMSRLFSKFL FKGEDTPFVM ELPPYRFPTA
KAIGRHTWQK GKEYLKKMGG IILVASLIVW ALGYFPHNDQ LTKQEQQEQS FIGHIGHAIE
PVFRPQGFDW KLDVAVVSGV GAKEIVASTM GILYTSDDAA EEGSEQAYRH LEHQMLADGI
TPLVAYSFLV FVLLYFPCIA TIAAIKNETG SWKWAAFAAT YTTLLAWVVS ALVYQIGKLI
V
//
