ID G5IDI2_9CLOT Unreviewed; 1126 AA.
AC G5IDI2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Fragment;
GN ORFNames=HMPREF9473_01559 {ECO:0000313|EMBL:EHI60428.1};
OS Hungatella hathewayi WAL-18680.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=742737 {ECO:0000313|EMBL:EHI60428.1, ECO:0000313|Proteomes:UP000005384};
RN [1] {ECO:0000313|EMBL:EHI60428.1, ECO:0000313|Proteomes:UP000005384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL-18680 {ECO:0000313|EMBL:EHI60428.1,
RC ECO:0000313|Proteomes:UP000005384};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA Molitoris D.R., Song M., Daigneault M., Allen-Vercoe E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium hathewayi WAL-18680.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EHI60428.1}.
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DR EMBL; ADLN01000020; EHI60428.1; -; Genomic_DNA.
DR RefSeq; WP_006779545.1; NZ_JH379027.1.
DR AlphaFoldDB; G5IDI2; -.
DR HOGENOM; CLU_000445_114_21_9; -.
DR Proteomes; UP000005384; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000005384};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 64..113
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 116..167
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 199..244
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 247..298
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 462..593
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 787..1008
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1032..1126
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1084
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 1126
FT /evidence="ECO:0000313|EMBL:EHI60428.1"
SQ SEQUENCE 1126 AA; 127046 MW; 37D5A204ACE7B2F4 CRC64;
MDTDYTEQPN TAHSGNRQPE EYFPAAPLNR SVQEHNVGAK SLDILGQNLP GGMIGGYLEP
GFPLYYVNDY MLSYLGFTFE EFVAAIDGLV INCTHPDDRE RVGLTVDKAF EAGKPYEVQY
RMLKKDGSYL WVNDVGKKAV AEDGRQICIS VIRDISAEKE YQERLEKQAA HYDHLFHSVL
TGIVQYRMVD GAVEFKNANQ EAIRLFGYTP EEFWSKRDWD LASLIAPEDR DRVLAEVERL
RQPGDMNPFE YRMIQKDGNQ CWIIGRAEMI IDTDGEQVIQ SVFLDINEQK MAEQQNERLT
EQVEASNEIL HLALEHTNTC EIYYYPQTGT CLVPERTCNI YKCETRYTDM PGSFAEAQVD
EEFRPAFYEM YKRIHRGEHT ASCEFRGGNG SYWCRQTLSV IRIDKNGAPQ LVIGILEDIN
RQKEMELALL EARSRDRLTG LYNRETGIQM IQDYLSRRPA REHGMLVLLD MDDFDIINQK
EGRVFADAVL QETADLLKAE TKPDDILIRL GGDEFMLFLK KRDRKTASQT GVRLARLARN
ILEKTERDIQ VSVSVGMCST EAAGDYNTLY RCAASTLKFV KENNKGTACS YLDAQIADAR
LAQIDTEEHL INEIETGSSL ADGDLGSFAL DLLGKTKSLD DAVSLLLARV GKTCGFDRVS
IIEANRAYLT YRFSYQWARR RSDLQLGQDF YVSEEDFELC SAMYDEDGLA DHNLRDGISN
IASCLHAGIW DYGEYVGSMS FEVDKKGFVW TKEHRKLLME LVKIVPSFIM KSKADAISQA
KTDFLSRMSH EIRTPMNAIS GMTTIAKSVV HDSAKTLDCL EKIESSNVYL LNLVNDILDM
SRIESGKLEL NYGALDLSQL LESLNSLFHA QAQEKGLSMR LEDGRVRNRL LRADSLRLNQ
VLVNMIGNAV KFTSQGGITV RVEELETEPK AVYRFSVMDT GCGIEPSSLS RIFNPFEQAD
ASTASRQGGT GLGLSISYRL VQMMGGILEV QSEVGKGSRF FFTLAFSYAP EEVSEQADTK
TPVSLPDFHG RRILLAEDNE LNREIAQTLL EMNGLTVECA ANGQEALEFF CSEEPGRFDA
ILMDIRMPVM DGLEATRRIR TCGHPDARTI PIIALSANAF DEDSKK
//
