ID A0A416EDL0_9FIRM Unreviewed; 1067 AA.
AC A0A416EDL0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, 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=DWZ56_16720 {ECO:0000313|EMBL:RHP31292.1};
OS Lachnotalea sp. AF33-28.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnotalea.
OX NCBI_TaxID=2292046 {ECO:0000313|EMBL:RHP31292.1, ECO:0000313|Proteomes:UP000285302};
RN [1] {ECO:0000313|EMBL:RHP31292.1, ECO:0000313|Proteomes:UP000285302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF33-28 {ECO:0000313|EMBL:RHP31292.1,
RC ECO:0000313|Proteomes:UP000285302};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RHP31292.1}.
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DR EMBL; QUEE01000013; RHP31292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A416EDL0; -.
DR OrthoDB; 9803190at2; -.
DR Proteomes; UP000285302; 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; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.10.450.50; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR032710; NTF2-like_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 InterPro; IPR037401; SnoaL-like.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF13474; SnoaL_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000285302};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 213..264
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 349..400
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 561..784
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 805..925
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 942..1063
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 117..144
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 859
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 994
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1067 AA; 120759 MW; 218067F537169695 CRC64;
MEPLFDSFAQ DIVWLGAGEA QHAEGRDAVK AQFLAGKDDM IPFDMWDEWY VVRPLGTDCY
LCEACSMIQA KEGTGMSLKE CQRVTFIFVR IQGQLKTVHI HNSVAYKALR KDELFPVEAA
SNAYKRLQEQ LDLQERQIDL MLSQLPGGMA MICPDENFTV KWISEGLCRL LGYQDMRGYM
EQSGGWFRSV VSEEDYETMC RNVKESLAAG GAYSAEYRIM RSDGEILWVM DVGKMIKDEN
GAGILSCFIT DITARKTQES ELLAANREVA QQAAFLTQLY NTVPCGIIQF TTGPEHRIIH
ANRRAWEIYG YEEKEYWDRM VSPFDSVLLK DKQHFTEIVD RLSGEGGSIS YEREGTRRDG
SLCYVSVYME RVVNADGYEV IQAVFNDITE KRLLEKEREQ EQLLENRILR AAIYTAYPMI
ISVNLSKDSF TSITPANFIT AHMSGGTYSR MVEKVRGSIK PTYQESLARF FSIEAIQKRF
LTSDQELYME VEQSEDDGVW HRVSAHVVHV ENPYGTDQLA IILYRILDEQ YAEKSRQEQL
LRDALAAAEA ANRAKSDFLS SMSHDIRTPM NAIIGMSTIG QLKADDPKRM LDCFRKIDAS
SRYLLSLIND ILDMSKIECG KMELTEEQFD FTEFINSLTS IIYPQADIRK LSFEVYHTEP
LDRFYCGDSL RLNQILMNLL GNALKFTPEG GRVTLKVMEE RRENQYAYLQ FTVKDTGIGI
SGEFMERIYK PFEQESLDVA RNQTGSGLGL SIVHNLTRLM GGTISVDSER GKGTLFVLSI
PFRLVDEAVS AAEHRGQKQL LKGNRVLVVD DDSIVGEQAA HILDGIGAFS TWVDSGRKAV
DEVGKAINEL RPFDLALIDW KMPDMDGVET TRQIRRLAGK DTMIIIISAY DWSDIEKEAI
EAGADYFIAK PLFASSVCST LCGLKLNRHS AENRTYHIQG RKVLLVEDNE MNREIARALL
EMQGVVVEEA QNGRIAVDKC REAAAGEYLA VLMDIRMPVM DGLEAARQIR ALEKHSAVRT
PIVAMSANAF EEDRAKAYEA GMDGYLIKPI EVDKLMETLQ RLEEAMP
//
