ID U5MUF4_CLOSA Unreviewed; 1155 AA.
AC U5MUF4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=arcB1 {ECO:0000313|EMBL:AGX43296.1};
GN ORFNames=CLSA_c23220 {ECO:0000313|EMBL:AGX43296.1};
OS Clostridium saccharobutylicum DSM 13864.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX43296.1, ECO:0000313|Proteomes:UP000017118};
RN [1] {ECO:0000313|EMBL:AGX43296.1, ECO:0000313|Proteomes:UP000017118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX43296.1};
RX PubMed=24285650;
RA Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA Gottschalk G., Daniel R.;
RT "Complete Genome Sequence of the Solvent Producer Clostridium
RT saccharobutylicum NCP262 (DSM 13864).";
RL Genome Announc. 1:e00997-13(2013).
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};
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DR EMBL; CP006721; AGX43296.1; -; Genomic_DNA.
DR RefSeq; WP_022746447.1; NZ_AYXL01000244.1.
DR AlphaFoldDB; U5MUF4; -.
DR GeneID; 55476838; -.
DR KEGG; csb:CLSA_c23220; -.
DR PATRIC; fig|1345695.10.peg.2307; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_15_9; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000017118; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 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; 5.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 4.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 5.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Membrane {ECO:0000256|ARBA:ARBA00022519};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000017118};
KW Transferase {ECO:0000313|EMBL:AGX43296.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 10..83
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 88..140
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 284..354
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 357..409
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 406..449
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 473..525
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 526..601
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 671..892
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 916..1030
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 965
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1155 AA; 131403 MW; A8E54AB2CADAEB86 CRC64;
MIEKKIIDRK NYFLSATLSS IGDGVLATNL SGNITFFNKA AEEITGWAIE EVIGKSFQNI
FTLVDINTKK ALEDPINNVL EFYISTGLDE NSALITKNKE IKYISATISP IKDDNGIVLG
SVTVFKDITK IRSMVLKNKE EQSDFIRLFN SAPVGAIVLD ENSVISKINE VASEFLDSNN
ILRIGKKFGD ALGCEESFTN EQGCRYGSQC NNCDIKKATY LALNAGLSTN NIEFSRVFNI
NGMKKKLWFK ASVTPVIQEN KKNVAIAFID ITDRKKAENE IAKSRDYYLG MFENFPSMVW
KTDSSGKNEF VNKKCCDFTG KPREECFGDN WISIIHPEDR KRCYEIKTKS LQERKSYEIK
YRAMNSSGIY RVIKSIYRPF YNLEGKFDGL IGTGIDVTDK KNAEEWLNRY KILSESVRDI
IHFIDIEGNI IDANQSALRA YGYTYEEILK LNIRDLRAEG IITRELMDKC YKYGIFYETL
HKYRDGNTFP VEISAKGANI AGKRVIISII RDITERKQIE TTIREREEKY RNIFNNANDA
IYVYEINNDF KYEKFIEVND VACTYLGYTK DELLNMSFYD INGEKTKEII DEKVDIVRRN
GKGIFETCHR TKENRIIPVE VNVHTFNQNG KRVALAIVRD ITQRKMVESS LKLAKKSAEI
ANKTKSEFLA NMSHEIRTPI NGIIGMVDLT LATELGNEQK ENLMIVKSCA NSLLRVINDI
LDFSKIEARK LVIENINFDI KSLIAETIKV HSPGAIAKDI ELNYAFSSIT PQYVIGDPSR
LQQILNNLIS NAIKFTDRGE VWVKVKQIKS KNDEVYLKFS VEDTGIGISE DNIGMLFKSF
SQLDGSITRK FGGTGLGLAI SKQLSEMMGG KLWVESKKGL GSNFYFTLKF DIGEKIKPQS
KEKIQFQPTN IHTLHNILLT EDDEVNQMVI TRMLRERGYF VDIANNGLEA LEMCKKKLYD
VILMDIQMPV MDGIEATKII KEINKSIPII AITAYALKGD GKKFLSQGMD GYISKPINAE
ELYSTIEETL FLNKYNENLS GVGICLDENG DIVLKQKEAP IFDKKNSEKL NRLSKEIKAI
NNTLDKKEFF LIESLANKIK NLSNEIGIEE LKTTAFKIEL DARRGNFEQL TNKVQRANSI
FQAFKKSVLQ EEESI
//
