ID R5JT86_9CLOT Unreviewed; 880 AA.
AC R5JT86;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BN743_01079 {ECO:0000313|EMBL:CCY57778.1};
OS Clostridium sp. CAG:632.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262830 {ECO:0000313|EMBL:CCY57778.1, ECO:0000313|Proteomes:UP000018242};
RN [1] {ECO:0000313|EMBL:CCY57778.1, ECO:0000313|Proteomes:UP000018242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:632 {ECO:0000313|Proteomes:UP000018242};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- 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:CCY57778.1}.
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DR EMBL; CAYL010000021; CCY57778.1; -; Genomic_DNA.
DR AlphaFoldDB; R5JT86; -.
DR STRING; 1262830.BN743_01079; -.
DR Proteomes; UP000018242; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF82; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE ARLS; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CCY57778.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000018242};
KW Transferase {ECO:0000313|EMBL:CCY57778.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 506..730
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 756..877
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 808
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 880 AA; 99770 MW; D5A76F4D0D3BB43C CRC64;
MTTDKNTDNY SRLQTKLNDF EILLQQMVFI DRAQDQNELN AATQALIRVI GDYTQANRVY
IFDKEPDSDT YRNSFEWCAP GIAAWIDNLQ AVSASKMPYW QSAFERGENI IIDDVESVKK
LMPSEYAMLK IQDIQTEIAF PIYSQNQLCG FIGLDNPQIA RSQSFISLLA VVGGHLGNAR
KNIRMAALLE QKRDSLQKSN HELEREKLYL SVLCIDYTSV YCVDLARETV EIIKLDSISN
IARETAFSQN RTLNYQTMLK SYYDQYVYKE TAPDFLEVLS IPNIKLSLSQ NNRLIYHYQS
IPNLAGQEYF EIQVVPLSDT LHESKVIIGF RHIDDIVKGE QAQQRKLQEA LDEAQLNNEI
ISAISKVYFA IYRIDLREDF YEEISSDNEV HRLTGRIGKA SAKMVELCDT FVAPAYHDSV
MKFFDLSTLA DRLKNDEVID IDYLAKDGNW HLARFIVKKR DEKGTVTHVL YVTRLISEQK
RREQNWIFIA EEANRANVAK SDFLSRIAHD IRTPMNAVLG FVDITKKHLN EPEKVKTGLD
KIQLAGSYIE QLVNDILDIA SIENGKMELH PETVNIADIL EDFSDTLQAS IVTKHLTYNC
KKHNIDHPYL TVDSLRLKQI YMNLLSNSIK YTPEWGSITF EFYEEPSATA GRTTLVAIIS
DTGIGIDPEY MEHMYQAFSR EVDTRVNKVR GSGLGLAIVK QLVDLMNGTI RVESTVGKGT
SFHIELELPY TTPSVSGESA EASDSPDPTT SCNGMHLLIA EDNDLNYEVV SELLRMYHIS
CERAENGAIC VDKFSASGPD TYDAILMDMQ MPVMDGPEAA QVIRTLTRPD AQTIPIIAIT
ANAFTRDIER CLAAGMNEHL SKPLNVHQLL AILDKYKSTA
//
