ID T1UB30_HELPX Unreviewed; 859 AA.
AC T1UB30;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=2Fe-2S iron-sulfur cluster binding domain protein {ECO:0000313|EMBL:AGT74580.1};
GN ORFNames=HPSA20_1369 {ECO:0000313|EMBL:AGT74580.1};
OS Helicobacter pylori SouthAfrica20.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1352356 {ECO:0000313|EMBL:AGT74580.1, ECO:0000313|Proteomes:UP000015920};
RN [1] {ECO:0000313|EMBL:AGT74580.1, ECO:0000313|Proteomes:UP000015920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SouthAfrica20 {ECO:0000313|EMBL:AGT74580.1};
RX PubMed=24072860;
RA Duncan S.S., Bertoli M.T., Kersulyte D., Valk P.L., Tamma S., Segal I.,
RA McClain M.S., Cover T.L., Berg D.E.;
RT "Genome Sequences of Three hpAfrica2 Strains of Helicobacter pylori.";
RL Genome Announc. 1:e00729-13(2013).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP006691; AGT74580.1; -; Genomic_DNA.
DR AlphaFoldDB; T1UB30; -.
DR KEGG; hpys:HPSA20_1369; -.
DR PATRIC; fig|1352356.3.peg.1332; -.
DR HOGENOM; CLU_021910_0_0_7; -.
DR Proteomes; UP000015920; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 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:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR PANTHER; PTHR24960:SF88; PHOTOSYSTEM I IRON-SULFUR CENTER; 1.
DR PANTHER; PTHR24960; PHOTOSYSTEM I IRON-SULFUR CENTER-RELATED; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..76
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 76..115
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 134..163
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 193..223
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 232..291
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 468..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 96053 MW; 033E5AAE9EB0C9AA CRC64;
MITMNINGKT IECQEGQSVL EAARSAGIYI PTICYLSGCS PTVACKMCMV EMDGKRVYSC
NTKAKNNATI LTNTPTLMDE RKSIMQTYDV NHPLECGVCD KSGECELQDM THLTGVEHQP
YAVADDFKAL DSWAKALYDP NLCIMCERCV TTCKDNVGEN NLKATKADLH APDKFKDSMS
KDAFSVWSRK QKGIISFVGS VPCYDCGECI AVCPVGALSY KDFAYTANAW ELKKIHSTCS
HCSAGCLISY DVRHFDTLGE ESKIFRVLND FYHNPICGAG RFAFDVSSSP KGSANLKEAQ
NALKECDAVR IGGDITNEEA FLIERLRKEL DFKIYNKDLY PFQQFLKVLG EIKRPSIEEV
KTSNLVITIG SSIKTENPLV RYAINNALKL NKASLIAMHP IKDNALANLC RSSFCITHEV
GAEEILLGML LKMLNIESAA LKSLEDSKQD IVDEAALKAL EEEKKKTLEQ ANQGCSLEEN
KAENEETTAE DKAENKEEDQ IKTATPKEEN KAENAENKEE NKTENTEKLP TKTTYLLLEE
AGINLETYEK ILALLQKSNN TLLVVGEEIY RHQQAHNIAK MLRLLAQKSA IKLILIPPSA
NALGIVSLCE LNEEIFEHEK IVGIRAQGDF TINSDEKVFG KDAVSAVDFI LPSLNQLEGT
ITNIEGRVLP LKPALRFEGY DLSDIMQGFG FVEENLIECT HKLPKEAGFK AIEFDHLTNY
FTNDRANHRG YELETSHFEK SAKECEETEC DPIKPLKEKI AFNAYLKYPE TQFNSATHKS
ENLQLKTGIY VSKAFLKKLN KEVGQHITLM KEEEELVGIL YLDESLDQEV FVISPSLLGN
DSNFFKESVF DSVDLKEQA
//
