ID S4Y3X9_SORCE Unreviewed; 1561 AA.
AC S4Y3X9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SCE1572_40175 {ECO:0000313|EMBL:AGP40182.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP40182.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP40182.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP40182.1,
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; AGP40182.1; -; Genomic_DNA.
DR STRING; 1254432.SCE1572_40175; -.
DR KEGG; scu:SCE1572_40175; -.
DR PATRIC; fig|1254432.3.peg.9084; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3899; Bacteria.
DR HOGENOM; CLU_000445_34_2_7; -.
DR OrthoDB; 5521237at2; -.
DR Proteomes; UP000014803; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 1..92
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1322..1537
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1533..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1561 AA; 173377 MW; B690DD05FE02E116 CRC64;
MNRAVDHRTD LYSLGVTFYE MLTGARPFHA EDPLEWIHCH IARSPVPAAQ RVPGVPHVVS
DIVMKLLSKV AEDRYQSARA LAADLVRCHA ALGAKAGVNG ACMENGIGAW VEPFPLGERD
VSDWFQIPQR LYGRDADVAA LLRAFERVAA GATPELMLVS GYAGTGKSTL VNELNKPIAR
ARGFFISGKA DQYTQNTPYS TIVQAFRELV LELLAQSEAQ LGRWRERLKS ALGANAQIII
DVIPYIALIL GPQPPVPEIP LTEAQNRFNM VFRRFINVFA QRDHPLALFL DDLQWADPAS
LKLLHDVVTN PDTKYLLTIG AYRDNEVTPS HPLMLTLEEM RRAGVIIHDI VLSPLSPRDL
ASLVADTLRC RSEAAEPLSE LVYAKTAGNP FFAKQFLSTL HKDALIEFDP EPAAWRWDVQ
QIRARNFTDN VVDLMVEKLR SLPAATQDAL KIAACMGAAA DVRTLAAIHK LSEQEILPVL
WDAVQEGLLV LQGDACRFVH DRVQQAAYQL IPDALRREVH LTIGRLLLSR APREALEEQV
FDIVGHLNIG ASLISSQDER YSLAEFNLVA GKRARATTAY ASAASHLEAG IALLAHDSWD
TRYELTYGLH LLRAECEHLN GSFEEAGRLL SLVLRRAKTP IDVMSASSVK VYNHTIQEEN
EEALQVGIDC LRLFGIDLSL HPTREEVHRK CEKIWRDIGD RRIKDLIDLP IMTNANAKAV
VNFLATLHAP ALFFDSNLLC LLLCHQVELS IQYGNTDGST IGYVFFGVVP GPMFGKYREG
YEFGELGYAL VEERGLTRYK AKVYVEFAIL IRPWTHHLRS ILDILRRAFD AAVEVGDLTY
ACYAQLSTIT LLIVRGDPLD SVYRESERAL DFARRARFAA VEHIIIGQQR LIQNLRGLTR
SFSSYSDAQF DQDEFEDYLT RNKARVPLAA LHYFVWKTQA RFMSGDYKQA LHSAGQAKDL
LWVSPVSLES AEHCFYDALT LAACCEEGAP DERSEHLEKL AAQEERLREW ESSCPENFLY
KHALLAAEIA RITGEDHEAM RLYERAIRAA KENAFVSGEG LCLELASRFY RERGFEAFAD
TYLREARHCY LRWGANGKVR QLEQQHPELA PSAPSAANAT FAARAEHLDL VSVVKASQTI
SGEIVLERLI RRMIQVVMEE GGAQRGCLLL ARDGILQIEA EARLDEGGLA TTMLGSIPAS
SSSLVPTSIV AYVWRARQPV ILADATREIE VGKFSSDEYL ARARPRSVLC VPIVRQTEPI
GILYLENNLA AGAFTADRLA ILEVLAAQAA ISLENALLVL REHEARVAAE DALRLREEFL
AVASHELRTP LTPLRLQLQR VHRTLTRQNL HALAEQIERP LRQVDRLTAL VVNLIDVAQL
SNSQLVLRLQ PVDLAALVRR VVADYRDALH QSGCALELNA GAPVIGRWDA ERIEQVVVAL
LSNAMKYGAG RPIVVAVVAE GALAKLSVRD LGIGVAAEDR DRIFGRFERA VSVQHYGGLG
LGLYIARQIV LAHHGTIRLE SEPREGATFI VELPLAPPGG PGEQDRPPAA QPRGGEVSED
P
//
