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Database: UniProt
Entry: I0XPP5_9LEPT
LinkDB: I0XPP5_9LEPT
Original site: I0XPP5_9LEPT 
ID   I0XPP5_9LEPT            Unreviewed;       755 AA.
AC   I0XPP5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase / 4Fe-4S binding domain multi-domain protein {ECO:0000313|EMBL:EIE00853.1};
GN   ORFNames=LEP1GSC185_0511 {ECO:0000313|EMBL:EIE00853.1};
OS   Leptospira licerasiae serovar Varillal str. VAR 010.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE00853.1, ECO:0000313|Proteomes:UP000004889};
RN   [1] {ECO:0000313|EMBL:EIE00853.1, ECO:0000313|Proteomes:UP000004889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VAR 010 {ECO:0000313|EMBL:EIE00853.1};
RX   PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA   Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA   Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA   Vinetz J.M., Matthias M.A.;
RT   "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT   Leptospiral Evolution and Pathogenicity.";
RL   PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
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:EIE00853.1}.
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DR   EMBL; AHOO02000011; EIE00853.1; -; Genomic_DNA.
DR   RefSeq; WP_008595843.1; NZ_AHOO02000011.1.
DR   AlphaFoldDB; I0XPP5; -.
DR   PATRIC; fig|1049972.3.peg.3000; -.
DR   OrthoDB; 9778740at2; -.
DR   Proteomes; UP000004889; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR48105:SF33; OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF12801; Fer4_5; 2.
DR   Pfam; PF13187; Fer4_9; 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        372..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        414..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        439..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        469..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        539..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        601..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        635..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          681..710
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          712..741
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   755 AA;  84258 MW;  BDB7C2E1B07371C8 CRC64;
     MSLLSFVPKY FDWLNNDAPQ GESEKYPETN SEFESSIPGI YISGDLTGVP LLKYSVKSGV
     SVIQSILRKP KKKTKGNLDV LIIGAGPSGI AAGIEAKKNG LDFLILEANQ PFHTITSYPK
     GKPIFAEPSE LKVDSPIQIK DTTKEDLLKS LEKVLKKHKL PILNGEKVEM IQPSRGSEQG
     FEIRTESGKQ FHTTYVVLAI GKSGDSRRLG IPGEEQENVF HRLIDPQDFR GQNTLVIGGG
     DSAIEAALSL VDVSSSVTLS YRESEISRPK EENKRKFEKA IKENKIRFVP NSTLQKFGSK
     QVLIKQGSKT RTEKIDSSLV LIGSEPPLSF LERIGIKIRN SLNSKEVIGF VSLFSFALFL
     YFGKASFYAS FWYSWVALGS GIVFALSSVR FLFSKGTFSS LRWRTFKNLY LLSAALYFSA
     VYLSAKYLGF YLFGKYPNFH YTVLYSATIL FFGIRRIQVR PTQYIKLQTI TLILIQIFPL
     FLLPEIILPF LGDKGILGPS NGFLLTQVFP DGAYWKAYGF ILAWPLNMGV LYDGGITTFW
     LIYGFLMSFG LIPYLVYKFG KGAYCGWICS CGGLAETLGD EYRNRMPHGK LAYKLEHSGQ
     WILLIAAILT VAKLIGSSGQ FFWPLEFGAD SVKVYYDLIV DLGLGGVVGV GAYFMFSGRI
     WCRMFCPLSA LMHIYAKFSK FRIFSEKKRC ISCNICTSVC HQGIDVMNYA NKGRPMDSVQ
     CVRCSACVVN CPTQVLSFGK LEKSGQVLDT LKAVL
//
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