ID A0A1G5GR93_9FIRM Unreviewed; 1054 AA.
AC A0A1G5GR93;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN02910292_02011 {ECO:0000313|EMBL:SCY54102.1};
OS Lachnospiraceae bacterium XBB2008.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520826 {ECO:0000313|EMBL:SCY54102.1, ECO:0000313|Proteomes:UP000199089};
RN [1] {ECO:0000313|EMBL:SCY54102.1, ECO:0000313|Proteomes:UP000199089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XBB2008 {ECO:0000313|EMBL:SCY54102.1,
RC ECO:0000313|Proteomes:UP000199089};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMVL01000007; SCY54102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5GR93; -.
DR STRING; 1520826.SAMN02910292_02011; -.
DR OrthoDB; 9813048at2; -.
DR Proteomes; UP000199089; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SCY54102.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199089};
KW Transferase {ECO:0000313|EMBL:SCY54102.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 354..575
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 724..841
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 879..980
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 884..911
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 773
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 918
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1054 AA; 119883 MW; A49FFB1D6FEBF8BC CRC64;
MNIVLAGILI LLAMIGVLFY KLAYKGRVKA VNDALSFVCG VGVATMVCCA VLTVSANKNM
VMGMYTFYYI FYAMTLFAFA RFAYVFCTGS DRDLFRSPLF YGTVMVVLMM LNNLFTHDCF
TVTVYDFNGY VFPKTVHQGI FFLYASFMVM ESLIAALYLI SAYIRSAHTY RPRYIMILMV
IIFHLGLEYL SSYLDLPTAI KTCFLLPEGL LLAYLCSYYS TRRLTMAVLN FVTDNSTTGL
MIYDEDDYLI YHNKKIDEIL TGEQIREFYE IENMNRWSSD LEEINEIYIK RVEIDGETKY
YNIFKREFTE GDSYIGTSFS FHDTTEALER FAMVEEANEE LKRAAHMKSD FLANMSHEIR
TPMNAVIGLA EMALREDMTD QARDYLGQIK SSGRNLLNII NDILDFSKIE SGKMDIIPEP
YEPLSEFNDV ANTLITRIGD KDIELTMEEN PGIPCKLEGD VLRIRQILIN LANNAIKFTH
RGRVQIISDF TPIDNENIML RFHVVDTGQG IKKEDLKKLF NSFQQVDSKR NRSIEGTGLG
LAISKSLVET MGGSIGVESE YGKGSDFFFE IPQKIVDATP SISVNQPENI FALGRLNKKY
LARRFFIDCS KMGVFNVVLR YCEDYESTCD LYADTIEGKR KYIFFEECDY RDGVRDLLIN
DPELIGVMLA EFGSAVKPDL KNVRIIKKPF STAAIAMALN NMELHLNNED GKAYVSDFTA
PDAKILIVDD NMVNLTVAEG LLEPLKMKVV CATSGKEAIE KINIERFDIV FMDHMMPEMD
GVETTHVIRR MYPELAEMPI IALTANAVSG VKEFFLKEGM NDFVPKPIEI RDIMTKVRQW
LPEDKIKKGY KIVDVDSDED DEIDIPGLDV HSAMAMIGSP KLYIKILKEY YRNIETNHKQ
LEEAYESQNW EDYTIKVHAL KSSSRQIGAK DLAGKAEALE NAGKAGDIDY IRNNSQEALD
EYIALEALLH DHCADEDDAG AKPQIEADTL KTILDKTIAA CDELDMDAME SIVEELRRYS
YSDEIQADID SMIESAELMD VFTCKEIAEK LLDM
//
