ID W3AKS5_9FIRM Unreviewed; 1024 AA.
AC W3AKS5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=UYO_2648 {ECO:0000313|EMBL:ETP71393.1};
OS Lachnospiraceae bacterium JC7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1165092 {ECO:0000313|EMBL:ETP71393.1, ECO:0000313|Proteomes:UP000018967};
RN [1] {ECO:0000313|EMBL:ETP71393.1, ECO:0000313|Proteomes:UP000018967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC7 {ECO:0000313|EMBL:ETP71393.1,
RC ECO:0000313|Proteomes:UP000018967};
RA Rosewarne C.P., Cheung J.L., Evans P.N., Tomkins N.W., Denman S.E.,
RA O Cuiv P., Morrison M.;
RT "Isolation and genomic characterisation of Lachnospiraceae sp. JC7, a newly
RT identified member of the bovine rumen core microbiota.";
RL Submitted (JUL-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:ETP71393.1}.
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DR EMBL; ALYD01000044; ETP71393.1; -; Genomic_DNA.
DR AlphaFoldDB; W3AKS5; -.
DR PATRIC; fig|1165092.3.peg.2607; -.
DR OrthoDB; 9813048at2; -.
DR Proteomes; UP000018967; Unassembled WGS sequence.
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; 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; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR019494; FIST_C.
DR InterPro; IPR013702; FIST_domain_N.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF08495; FIST; 1.
DR Pfam; PF10442; FIST_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ETP71393.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ETP71393.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 434..655
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 686..804
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 851..948
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 735
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 890
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1024 AA; 116439 MW; 39717191859C678B CRC64;
MIQRTFILFQ GDEMRTILKE WDQTIKDKPK DNMFLVFTVN GFTEEKLNSV LSLVVRDYPN
INMIGIHQRA SHKYNEYLRV SFCLMEKSVI TPFSYSFRDI SEDAAMGELS DRVKHISNPA
CILLFAAGSS TKISQQLGIF EKTHQIPVAG IWTADFENVE SETHYVWQNE KMRRGIVGVI
LSGKEILVHT EVLTGWRPLG KNFEVEVRNK GSEISIGETV VKKINGKNAI DIYSRYLNIK
PDEYLLDNIR EFPFLLKRDN ELISRIPYRY DEAGELYFLG HFRDDDIVSF SSGNKNSIFS
EIAYKVNRFA EFVPESSFLF GSDMRQIFKD KELKAFQNID ENIQYIRGKG QFLFHDGIGG
THNVSSVIMG IREGIPEDVK HVDYMDVLST TDNEGVVPLA DRTSTFLQAI TDDLNEAIAK
AESANKAKSS FLSHMSHEIR TPINAILGMD EMILREGVDS TVKSYALDIR NAGVELLGII
NDILDFSKIE SGKLTVIPIE YKMADMLRDL YHMIKKRADD KGLQLILEAD PEIPEVLYGD
EIRIKQIITN ILTNAVKYTE KGKVWFRIKI ENLNPMEVVL NFSVEDTGIG IKDEEKNKLF
EAFERLDEKR NRTIEGTGLG MNITQKLLKQ MKSSLNVESV YGKGSTFSFT LTQAVRSPSP
MGQVNIEERR ESYKKKGAAF IAPEARILAV DDTVLNLTVI KALVKQNHIN VDVAESGQEA
IELVKHNRYD IIFLDYRMPV MDGIETLHRM KELDGDPCMY TPFICLTANA VTGAIEEYMK
AGFDDVITKP IDAELLEKKL RFYLSPELIQ EEDIDEEEDM AEEPEDTGDL PAELKDVKEI
SIEDGLQHCG SAEGFMTALK SFYDSLKDNI RIIQENYDKA DIKNYTIKVH AMKSSARIIG
ANELSALAKD LEAAGDNEKM DVIVNDTPRL ISMAESLYAS LEPCFMVEEE DVSDLPELTE
DEWNDFIVTL GGFIEAYDID DLKMMLEMMK GYRLSKEYEI IYKDIKDAAK GPDWQKLSEL
VALK
//
