FEOAB_PORGI
ID FEOAB_PORGI Reviewed; 844 AA.
AC Q7MV19;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Fe(2+) transport protein A/Fe(2+) transporter FeoB fusion protein {ECO:0000305};
DE AltName: Full=Ferrous iron transport protein B;
GN Name=feoB1 {ECO:0000303|PubMed:15901729};
GN Synonyms=feoB-2 {ECO:0000303|PubMed:12949112}; OrderedLocusNames=PG_1294;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 53978 / W50;
RX PubMed=15901729; DOI=10.1074/jbc.m503896200;
RA Dashper S.G., Butler C.A., Lissel J.P., Paolini R.A., Hoffmann B.,
RA Veith P.D., O'Brien-Simpson N.M., Snelgrove S.L., Tsiros J.T.,
RA Reynolds E.C.;
RT "A novel Porphyromonas gingivalis FeoB plays a role in manganese
RT accumulation.";
RL J. Biol. Chem. 280:28095-28102(2005).
CC -!- FUNCTION: Probable transporter of a GTP-driven Fe(2+) uptake system.
CC {ECO:0000269|PubMed:15901729}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells do not transport Fe(2+). Cells are
CC avirulent and therefore unable to cause lesions in mice.
CC {ECO:0000269|PubMed:15901729}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FeoA family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class
CC TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC
CC 9.A.8) family. {ECO:0000255|PROSITE-ProRule:PRU01048}.
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DR EMBL; AE015924; AAQ66370.1; -; Genomic_DNA.
DR RefSeq; WP_010956271.1; NC_002950.2.
DR AlphaFoldDB; Q7MV19; -.
DR SMR; Q7MV19; -.
DR STRING; 242619.PG_1294; -.
DR TCDB; 9.A.8.1.6; the ferrous iron uptake (feob) family.
DR EnsemblBacteria; AAQ66370; AAQ66370; PG_1294.
DR KEGG; pgi:PG_1294; -.
DR PATRIC; fig|242619.8.peg.1196; -.
DR eggNOG; COG0370; Bacteria.
DR eggNOG; COG1918; Bacteria.
DR HOGENOM; CLU_013350_3_0_10; -.
DR OMA; PLGYDWK; -.
DR OrthoDB; 304844at2; -.
DR BioCyc; PGIN242619:G1G02-1201-MON; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR CDD; cd01879; FeoB; 1.
DR Gene3D; 2.30.30.90; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR008988; Transcriptional_repressor_C.
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 PRINTS; PR00326; GTP1OBG.
DR SMART; SM00899; FeoA; 1.
DR SUPFAM; SSF50037; SSF50037; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00437; feoB; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51711; G_FEOB; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; GTP-binding; Ion transport; Iron;
KW Iron transport; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..844
FT /note="Fe(2+) transport protein A/Fe(2+) transporter FeoB
FT fusion protein"
FT /id="PRO_0000210839"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..806
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 817..837
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 126..289
FT /note="FeoB-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT REGION 1..73
FT /note="FeoA"
FT REGION 74..844
FT /note="FeoB"
FT REGION 79..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT BINDING 158..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT BINDING 179..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT BINDING 240..243
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT BINDING 269..271
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
SQ SEQUENCE 844 AA; 94623 MW; B367AD5ED6360906 CRC64;
MRLSELHTGD QAVIVRVEGR GVFRKRILEM GFVHGKTITV VQCAPLRDPV YYRIMDYNVS
LRREDAAKIE VELISSNATS SPASNDIGEQ SANPDSNESI PTNPTEDISA KTKSEIEIEV
KPNGHVIRVA LIGNPNCGKT SIFNRASGAH EHVGNYSGVT VEAKEGLFRH GDYKIEIIDL
PGTYSLSPYS PEELYIRQYL SEETRPDLVL NVVDTCNLER NLYLTLQLKE MGLPVVIALN
MFDEFEKKGD TFDYPALSAM LGIPMVPTVG RTGQGLPELF DTLISIHEGR NKIIRPIRIN
YGSIIEPAVE ALTEKINNQL SLPYSLPARY IAVKLLEGDK EMNRFVGEQP KGLFILSARD
FALREIDEHL TVARDAESII TDQRYGFIAG ALKETYRSSY KQLKTLTDKI DHIVTHRVLG
FPLFLLFMFI MFEATFVLGR YPMDWIEAGV GWIGSMVNTF MPDGSFKDLI VDGVIGGVGG
VIVFLPNILI LYFFISLMED SGYMARAAFI MDKIMHRMGL HGKSFIPLIM GFGCNVPAIM
ATRTIESKQS RMITMLVTPL MSCSARLPVY LLLAGAFFPD SAGLVLFGLY FLGILLAVLL
ARLFKKTLFK VEDVPFVMEL PPYRMPTSRS VIVHMWNKAA QYLRKMGSII LLASIVIWFL
SYYPRYSEEA VLISQIEQIE GNPQLDEEKK TSQIEELNRK AHIEQQEQSY IGRFGKAVQP
VLAPIGFDWK MSVSLLTGMA AKEVVVSTLG VIYTGDSDDS DEAARRLGER IREDRDAEGN
HTFSPIIALA LMAFVLIYFP CIATVVAIGR ESGHWKWAVF SIIYSCSLAW IVSFLIYRIG
ILFF
