ID A0A2K9P2Z7_9FIRM Unreviewed; 1065 AA.
AC A0A2K9P2Z7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=B9O19_01439 {ECO:0000313|EMBL:AUO19600.1};
OS Monoglobus pectinilyticus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Monoglobus.
OX NCBI_TaxID=1981510 {ECO:0000313|EMBL:AUO19600.1, ECO:0000313|Proteomes:UP000235589};
RN [1] {ECO:0000313|EMBL:AUO19600.1, ECO:0000313|Proteomes:UP000235589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14 {ECO:0000313|EMBL:AUO19600.1,
RC ECO:0000313|Proteomes:UP000235589};
RA Kim C., Rosendale D.I., Kelly W.J., Tannock G.W., Patchett M.L.,
RA Jordens J.Z.;
RT "Monoglobus pectinilyticus 14 draft genome.";
RL Submitted (APR-2017) 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};
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DR EMBL; CP020991; AUO19600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9P2Z7; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000235589; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 1.
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; 3.40.190.10; Periplasmic binding protein-like II; 4.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 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; SSF53850; Periplasmic binding protein-like II; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AUO19600.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000235589};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:AUO19600.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1065
FT /note="Stage 0 sporulation protein A homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014765847"
FT TRANSMEM 502..525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 696..920
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 944..1065
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 996
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1065 AA; 121657 MW; 8F966EE94A89DECB CRC64;
MKRFVSIFLL FTLCLINLTV FSDENSHQKQ TLKVGFYQID FYQELNDSGD PSGYVYDYLS
KVGQYAGWDF EYIKAPFADC LNMLENGQVD IVCGISKNRE DAYKYDFSKY EMSTAAYELY
ASSAREDMNF DNLGKTADLK IGILEGSRHN YQLDDYINKY GYTYQPIYFK TQFEMQNALF
SNQIDLIYTI GSGSKKNLKV ITRFPEMPVY FALTKGSPYL NKLDNILFEM KNISPAFSYQ
MHKKYFNNGQ IFQPNFTQQE IDFINSSPEF KVVYDPYWAP IEYYDTNNKK YSGISADVLQ
LISKYSGLKF TIIDAPSYEE ACRMINEGEA DIISGITYDY NWASEHNVSL SNPYLNSNII
QIKKIEESNK NTIALPKGFY INKFIREKYE STSAIIEYDT IEECFDAVEN GNVNCTYANS
ITANYLLSKF KYSDLVSNDL TGSIQDISIG VSDTADPTLL RIIDKSLLSI TNGQIDNIIV
KNNNIYDDSY NLKTLFHSYP DMMTLLLSII ILFLIIFFIC FFIIVKNKIK AKRTANDVIL
GKVLMSMYDQ VWRVTYNNTS SNVEVINRNG VSNSCNFEFG LKKYIEYICL NNIHPNDRKN
FLEYFSDVNM SKLFCGESFS FEARTCKQDG KYSWYMYFVE SIHDDNKTKS GCKCILIANR
NIDETKKRQI EYENGLRDAL IVAENSAKTR DKFLRNISHE IRTPLNAIIG FTNLSKQNID
DKVKLNNYLQ KTEYASKHLL SLINDILDLS KIDSGKLQTK TEKFVLKDAV DELLAAINAQ
TEEKNIDLKI SFDKRLSGLA LIGDSLRFKQ IMLNILSNAV KFTGKNGKIE FDILRRSEVD
NILYISFIIT DNGIGMTDEF KDRIFTPFEQ QDERISREYG GTGLGMSIVK NLVTLLKGSI
NIKSKSGSGT SVTVELPFKY ENNQTKLSKN DHSENSEKSI AGKNILVTED NALNREIISE
LLKSQNANVE LAVDGLDAVK KYNNSADNYF DLILMDVQMP NLDGYEATAQ IRNSEKPDAV
TIPIIAITAH SFESDITKAL SSGMNAHISK PINVDDMFKT LHKYI
//
