ID I4A8V1_DESDJ Unreviewed; 974 AA.
AC I4A8V1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN OrderedLocusNames=Desde_1999 {ECO:0000313|EMBL:AFM00386.1};
OS Desulfitobacterium dehalogenans (strain ATCC 51507 / DSM 9161 / JW/IU-DC1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=756499 {ECO:0000313|EMBL:AFM00386.1, ECO:0000313|Proteomes:UP000006053};
RN [1] {ECO:0000313|Proteomes:UP000006053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51507 / DSM 9161 / JW/IU-DC1
RC {ECO:0000313|Proteomes:UP000006053};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA de Vos W.M., Smidt H., Woyke T.;
RT "Complete sequence of Desulfitobacterium dehalogenans ATCC 51507.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFM00386.1, ECO:0000313|Proteomes:UP000006053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51507 / DSM 9161 / JW/IU-DC1
RC {ECO:0000313|Proteomes:UP000006053};
RX PubMed=25512312; DOI=10.1128/JB.02370-14;
RA Kruse T., van de Pas B.A., Atteia A., Krab K., Hagen W.R., Goodwin L.,
RA Chain P., Boeren S., Maphosa F., Schraa G., de Vos W.M., van der Oost J.,
RA Smidt H., Stams A.J.;
RT "Genomic, proteomic, and biochemical analysis of the organohalide
RT respiratory pathway in Desulfitobacterium dehalogenans.";
RL J. Bacteriol. 197:893-904(2015).
CC -!- FUNCTION: May play the central regulatory role in sporulation. It may
CC be an element of the effector pathway responsible for the activation of
CC sporulation genes in response to nutritional stress. Spo0A may act in
CC concert with spo0H (a sigma factor) to control the expression of some
CC genes that are critical to the sporulation process.
CC {ECO:0000256|ARBA:ARBA00024867}.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP003348; AFM00386.1; -; Genomic_DNA.
DR AlphaFoldDB; I4A8V1; -.
DR STRING; 756499.Desde_1999; -.
DR KEGG; ddh:Desde_1999; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_9; -.
DR Proteomes; UP000006053; Chromosome.
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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00156; REC; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 19..132
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 209..266
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT MOD_RES 67
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 974 AA; 108557 MW; 4C02185828276EF9 CRC64;
MLSQESIHNN IRKKSGKYIC FLLEKNTERG KYLRRLLQAE NLSVLSFYSR QEVLEKVNDT
TQVIIVDATD YGVDYAAFFA ELRQRSPGIA VVALLADSSR AYRQHMLSGG ADAALAIERA
DELLAAAVWH SARKNTSVFA SNDCVEQAKE GIQNVKEDLK LFERQFNRRA FLKGSAAAAA
VTGVTVASPG KMATKALAAG DGTASVKQEQ IFYGACRANC FGGCRLKITV RNGKVVKTQM
AEVPDKRYNR VCARGLTHTQ MMYSPDRLKH PLKRVGERGA GQWEQITWEE AIKTITDTWK
KIRTELGNNS IGFSHGTGSN GVLTNNGFHR LRNLMEATCF YCNYDSNHIV TIGQCLGIGP
NYNGNEMADL INAKTIIFFG ANITESQPQN WHFVKEAQEN GTKLICIDPV STTLAIRSDI
HVPIRPGTDA ALAMAMMNII IKNGWTDDTF IKKSSVGPFL VKESDGTYLR FSDLWPLPEG
EQDAIVVRDK DGNIGVPGRI PDPVIKGSYT VNGIKVTTAF DLLVNRVAEW TPERTAELCD
IPVDQLHEIT RIYATETPST IFTGFGPDHY VNGNHAYVAI FALGMITGNI GKPGASTGWP
FNLGFNINAG AISTAPGSPI GPTLPQVKIP YIVENKQYGG KPLELRSIYH VNTNPLGNFA
GRQELLQAYE KLELIVASDW RLTDTARYAD IVLPAAHWFE VEDIHSSGQT TWTAFQEKAV
EPPFECKSDW EMIRMLAEAM GYGEHCSYTD SEMLRMACEG PGPEAFGISY DKLKSEKVVR
GALPPGKTYL YGEDGVFKTA TGRVQFYFEN PQPDYLYDPV NQKINPDEER LPYFEPPREA
WPETVGSFTR KPLAEKYPLV YTSERNKLKT HTMFGHNPWL LELYPEPIVK VNPQDARQRG
IADGDYAKVY NDRGYVVLKV VFSSGVRPGM LVVPKGWQAD QFKEGHYSDL VGNLVDDYRL
NNNYFDTLCE MEKV
//
