ID S4YBS5_SORCE Unreviewed; 914 AA.
AC S4YBS5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SCE1572_49295 {ECO:0000313|EMBL:AGP41796.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP41796.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP41796.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP41796.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(2013).
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; CP003969; AGP41796.1; -; Genomic_DNA.
DR RefSeq; WP_020741689.1; NC_021658.1.
DR AlphaFoldDB; S4YBS5; -.
DR STRING; 1254432.SCE1572_49295; -.
DR KEGG; scu:SCE1572_49295; -.
DR PATRIC; fig|1254432.3.peg.11118; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG2461; Bacteria.
DR HOGENOM; CLU_000445_114_15_7; -.
DR OrthoDB; 5479234at2; -.
DR Proteomes; UP000014803; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 27..97
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 99..151
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 548..773
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 795..911
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 494..521
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 844
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 914 AA; 98985 MW; 865F29605879BE76 CRC64;
MQRPDAPTTA HAGGSMTEGG EPSATLEAEQ IQLLLDALPA LISYIDDEER YRIVNRAYER
WFGEDRSSLA GRHVREVIGD SAYAAVKPRI DAVLGGQPQD FESRLVYRRS GRRHVRIQYI
PHFGASGEVH GFFTLVADIS EQKRAEEARR FLADVTALLD PVLDRDTSYR RVAELAVTSV
ADWCSVHTIE PDGALRARVI AHADPAKAEV VSRLAQRSRI PPEAETPLHE VLHGGPGRLL
SEIPDSVFAG VARDAEHFAA LCALGCRSAV IVPIRGEECV LAALTLASAE SGRTYTAADL
AFAEELAQCI QVALQRMRLY DMARDAEAEA RRRFLAEQEA RRAAERAAQR MAGLQRITAA
LADALTCEAV AEVAVDQGAA AAGAYAGSIV VTAGDAIECL KAVGYGPETV ERFRRMAASD
GLPLVDPLRT GAPVWLRTRK ECAARYPDFA ATALTSTTAS LCCLPLLVQE RPIGALGLSF
AEPRPFDHEE QEFLLALSRQ CAQALERARL HEERAAIIER ERRVALENAR LYREAHEADR
RKDEFIAMLS HELRNPLAPI TTGLELLRMS TGDRGDRGDR GDRDDSQILA TLERQVKTIV
RLVDDLLDVS RITRGKIELK RERFDVGAVV ETAVESVRTL LAQRRHELVL SVEPGVLVHG
DRVRIEQIVV NLLTNAIKYT NPGGRVSLSC AASGGDAWIR VADTGVGISA ELLPRVFEPF
MQARRTLDRS QGGLGVGLTL VKRLAELHGG RVEAVSAGPG EGTAISVWLP LAGASADGAA
APSTEIPRSG AGALRVLLVD DNVDAAEGLR RILQLHGHTV AMAHDGPAAL EAARASKPEL
VLLDIGLPGM DGYEVVRRLR ADPELRGSYI AAVSGYGQDQ DRRRSREAGF DAHLTKPVAT
AQLLALVAEA APRG
//
