ID W1J2Q4_9GAMM Unreviewed; 771 AA.
AC W1J2Q4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Ferrous iron transport protein B {ECO:0000256|RuleBase:RU362098};
GN Name=feoB {ECO:0000313|EMBL:CDL84994.1};
GN ORFNames=XSR1_60042 {ECO:0000313|EMBL:CDL84994.1};
OS Xenorhabdus szentirmaii DSM 16338.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL84994.1, ECO:0000313|Proteomes:UP000019202};
RN [1] {ECO:0000313|EMBL:CDL84994.1, ECO:0000313|Proteomes:UP000019202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL84994.1,
RC ECO:0000313|Proteomes:UP000019202};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT 16338.";
RL Submitted (NOV-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}.
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:CDL84994.1}.
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DR EMBL; CBXF010000121; CDL84994.1; -; Genomic_DNA.
DR AlphaFoldDB; W1J2Q4; -.
DR STRING; 1427518.XSR1_60042; -.
DR Proteomes; UP000019202; 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; 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 NCBIfam; TIGR00437; feoB; 1.
DR PANTHER; PTHR43185:SF1; FE(2+) TRANSPORTER FEOB; 1.
DR PANTHER; PTHR43185; FERROUS IRON TRANSPORT PROTEIN B; 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 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:UP000019202};
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 284..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 326..345
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 352..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 389..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 423..449
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 513..531
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 666..687
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 726..744
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT DOMAIN 4..170
FT /note="FeoB-type G"
FT /evidence="ECO:0000259|PROSITE:PS51711"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
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 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-2"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-2"
FT BINDING 36..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 57..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 150..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
SQ SEQUENCE 771 AA; 84572 MW; 14B9B8EA1EE4B221 CRC64;
MMKHLTIGLI GNPNAGKTTL FNQLTGSRQR VGNWAGVTVE RKIGHFITHD HKVELVDLPG
TYSLTTISEQ TSIDEQIACH YILSGEADML INVVDASNLE RNLYLSLQLI ELGIPCIVAL
NMLDIAQNQR INIDVKALEQ RLGCPVIPLV STRATGIDAL KKAIDNYPQQ STPVRVEYPD
ALLQEITVLS DRITEKFNPQ QRRWLTLQVL EGDIYSREIS GLTQEQLAES QARLQEKQIT
EPDLMIAGAR YQTINELCLS VIDTRSAIPN KLTKTLDTVI LNRWLGVPIF LFVMYLMFVL
AINIGGALQP IFDGASAAIF IDGMQWLGYT CHFPHWLTVF LAQGIGGGIN TMLPLVPQIG
MMYLFLSFLE DSGYMARAAF VMDRLMQAMG LPGKSFVPLI VGFGCNVPAV MGARTLDAPR
ERLITIMMAP FMSCGARLAI FAVFAAAFFG KSGASIVFSL YILGIIVAIL TGLLLKYTIM
RGEASPFVME LPVYHVPHAK TLLLQTWQRL KGFVVRAGKV IIAASMFIGA LNSFSFSGKT
VDNINESALA SVSKVITPVL QPLGVHPDNW QATVGLVTGA MAKEVVVGTL NTLYTAENIT
QAPFNPDEFH LLDQLKDAVD ETWDSLKETL TLSALSNPIE ASKGDGNMDR GSMGTMSAKF
GSAISAYSYL IFVLLYVPCV SVMGAIARET SRGWMTFSIL WGLNVAYSLS ALFYQITTFS
VHPQSSLITI LAVVLFNILI FIGLRRARSR VTVTLNNAPD RSCACSDNSC H
//
