ID A0A161WYQ3_9CLOT Unreviewed; 1122 AA.
AC A0A161WYQ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=rpfC_1 {ECO:0000313|EMBL:KZL92218.1};
GN ORFNames=CLMAG_20270 {ECO:0000313|EMBL:KZL92218.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL92218.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL92218.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL92218.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-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 -!- 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:KZL92218.1}.
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DR EMBL; LWAE01000002; KZL92218.1; -; Genomic_DNA.
DR RefSeq; WP_066621538.1; NZ_LWAE01000002.1.
DR AlphaFoldDB; A0A161WYQ3; -.
DR STRING; 1121326.CLMAG_20270; -.
DR PATRIC; fig|1121326.3.peg.2017; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000076603; 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; 2.
DR CDD; cd00082; HisKA; 2.
DR Gene3D; 1.10.287.130; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR008979; Galactose-bd-like_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:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000076603};
KW Transferase {ECO:0000313|EMBL:KZL92218.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 442..659
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 699..816
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 869..1090
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 818..852
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 749
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1122 AA; 127820 MW; CF6B9733B8A71AB4 CRC64;
MNKSKVTVLR SAFLLIALVI SLSIIFIFGN KNAKSIAEKP VAKDGVLDLR NWDFKKKGIA
KLNGQWEFYY DKLLIPEDFQ NENKPIKTGL LNIPGSFSSY IYNGQLLDNQ GYATYRLKVL
TNNVEDLYAI KTEYIQTSHK LWANGRVVAE SGKVGKSKTE MVSKVAPAVG AFYDKTGEIE
IVLQTCNYYY GVPQIDTILL GTEAQISEYR AKHMGFDLFL FGSTLVAGIY NFALFLRRKK
DKATLYFSIV CFLVGLRTIL VDERLIYSVF PNMNYIFDIK LLLWTFFLYV PMLVLFINSF
YPNLLNKSVV KGSSIIGIVY FFVILMLPTI YYNGLIFPFE IISNFLLLYI LYKLVYRYIT
EGQKCEMVIV AIFLLFITRL NDILYEYSII QTGSYAPVGM LIFIFAQSYV LADRFSTTFS
NIEEMTEKLK SIDKLKDDFL ASTSHELKTP LNGIIGLSES LVSGIYDPSN NEQNETLELI
QASAKRLSNL VNDILDFSKL KNNDVNLYMR AVDIRQLTNI VIKSCKPFLR NKKLNIVNSI
GIDMPWAYGD ENRIQQILYN LIGNAMKFTH YGEIKISAIE KDNYLEITIS DTGMGIPKDQ
IYKIFEPYEQ VEGINKNYGG TGLGLHITKK LIHLHGGQIK VQSILNKGSK FIFTLPKSDY
LSRCKDESQV NLANQAEEPV GQIKEKEKNK FNNSKDNKRI LIVDDEPVNI KVLKNFLEYE
KYTVISADNG KEAINIVSND KELDLVILDM MLPDMLGYEI CSLLREKYSL LDLPILIMTA
DNRTESLVVS FECGANDYLR KPFERSELLA RVKTLIELKQ SVRKAINLQK EVANTTKQVE
VLSENFEENK RKLSEILEYD KLKNEFFANI SHELRTPLNV IWSSVQLLQS INIGNSQDGY
DVNKYLKIMN QNSLRLLRLI NNLIDTTKID SGYLSLNLIN GNIVYIVEEI TLSAADYIKS
QGIELIFDTD VEEKYMAFDV DKIERIVLNI LSNAIKFTEK NGTIFVNIYD LGDKIQLSIR
DTGIGIPEDK LDKIFERFVQ VDKSLSRRSE GSGIGLALVK SLVEMQGGTI HAKSKLGEGS
EFVVELPAKL VEEDGEVNAY SVYDSSNSKV ERIQIEFSDI YE
//
