ID W8UDP9_KLEPN Unreviewed; 772 AA.
AC W8UDP9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Ferrous iron transport protein B {ECO:0000256|RuleBase:RU362098};
GN ORFNames=KPNJ2_00355 {ECO:0000313|EMBL:AHM77135.1};
OS Klebsiella pneumoniae 30684/NJST258_2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1420013 {ECO:0000313|EMBL:AHM77135.1, ECO:0000313|Proteomes:UP000019586};
RN [1] {ECO:0000313|EMBL:AHM77135.1, ECO:0000313|Proteomes:UP000019586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30684/NJST258_2 {ECO:0000313|EMBL:AHM77135.1};
RX PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J., Bonomo R.A.,
RA Musser J.M., Kreiswirth B.N.;
RT "Molecular dissection of the evolution of carbapenem-resistant multilocus
RT sequence type 258 Klebsiella pneumoniae.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(2014).
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; CP006918; AHM77135.1; -; Genomic_DNA.
DR RefSeq; WP_002920508.1; NZ_CP006918.1.
DR AlphaFoldDB; W8UDP9; -.
DR KEGG; kps:KPNJ2_00355; -.
DR PATRIC; fig|1420013.3.peg.336; -.
DR HOGENOM; CLU_013350_3_0_6; -.
DR Proteomes; UP000019586; 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: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; IPR006073; GTP-bd.
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 PRINTS; PR00326; GTP1OBG.
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 282..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 309..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 426..447
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 511..529
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 664..685
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 692..711
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT TRANSMEM 723..742
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362098"
FT DOMAIN 3..169
FT /note="FeoB-type G"
FT /evidence="ECO:0000259|PROSITE:PS51711"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-2"
FT BINDING 24
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 35..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 56..59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
FT BINDING 149..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603373-1"
SQ SEQUENCE 772 AA; 83925 MW; F643B8D61A5F47C9 CRC64;
MQKLTVGLIG NPNSGKTTLF NQLTGARQRV GNWAGVTVER KEGIFATTDH QVTLVDLPGT
YSLTTISSQT SLDEQIACHY ILSGDADMLI NVVDASNLER NLYLTLQLLE LGIPCVVALN
MLDIAEKQQV RIDIDALAAR LGCPVIPLVS TRGRGIEALK IALDRHQANS DLELVHYPQP
LLREADLLAQ QMSAQIPTRQ RRWLGLQMLE GDIYSRAYAG DAADKLDIAL ANLSDEIDDP
ALHIADARYQ TIAAICDAVS NTLTAEPSRF TAAMDKVILN RFLGLPIFLF VMYLMFLLAI
NIGGALQPIF DAGSVAIFVH GIQWLGYTLH FPDWLTVFLA QGIGGGINTV LPLVPQIGMM
YLFLSFLEDS GYMARAAFVM DRLMQALGLP GKSFVPLIVG FGCNVPSVMG ARTLDAPRER
LMTIMMAPFM SCGARLAIFA VFAAAFFGQN GALAVFSLYV LGIVMAILTG LMLKHTIMRG
EASPFVMELP VYHVPHIKSL IIQTWQRLKG FVLRAGKVIV IVSIFLSALN SFSLSGKVVD
NINDSALASV SRVITPVFKP IGVHEDNWQA TVGLFTGAMA KEVVVGTLNT LYTAEDIQNE
EFNPQTFSLG EELLAAVDET WQGLKDTFSL SVLANPIEAS KGDGEMATGA MGVMGSKFGS
AAAAYSYLIF VLLYIPCISV MGAIARESSR GWMTFSILWG LNIAYSLSTL YYQTVSFSDH
PRYSLVCILA VVLFNVVLFG LLRRARSRVD VSLLATRKTP ASCCSSPAGD CH
//
