ID M1NB09_DESSD Unreviewed; 974 AA.
AC M1NB09;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=UWK_00394 {ECO:0000313|EMBL:AGF76979.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF76979.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(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; CP003985; AGF76979.1; -; Genomic_DNA.
DR RefSeq; WP_015402677.1; NC_020304.1.
DR AlphaFoldDB; M1NB09; -.
DR STRING; 1167006.UWK_00394; -.
DR KEGG; dsf:UWK_00394; -.
DR PATRIC; fig|1167006.5.peg.445; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_21_7; -.
DR OrthoDB; 9813024at2; -.
DR Proteomes; UP000011721; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 3.30.450.20; PAS domain; 3.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000011721};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 470..543
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 548..600
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 613..831
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 853..973
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 907
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 974 AA; 108350 MW; 79C262814C31DADF CRC64;
MAPQPLRRKI NRILSLVAVA IFFIVFLLTG VSEYRETRAE DTAVMRARID VARTLTRDVL
FHVDAMVQKV LQSHPNNPAT ILSQLASSHY FELHDDSFYV LDPQGRVSLI SEPYINYTGL
DFSAMISTKS TPKQQVQHHY KSLLTNRSVV TLQYPLDNGY LLVVERNLAN ITPVLASFED
GKLFPGELFF VLSTDGRTIY HPNRSLMETR HNLGFDLKEV SRPDSSGLFS FFYKGQKYIA
LSERFTEPDN WTIYYCIPNK VIMEKTQDFL IIQLLSLLFF FALLFCVFRI VFNRFFSRPV
NNIVEVLKHS GQGNRLTLSP DTSGGILEFE TIAGAISSRD EEIFKTAERF RILLDSLDAL
VYVADMETYE LIFVNSYGRK IYGEAVGRKC YEALQKGQDA PCEFCTNHLL VDSDGKPTKV
HIWEFQNTLT GQWYQCRDQA VYWTDGRLVR MEIATDISDR KDSEDALQAE KERLSVTLRS
IGDGVITTDV EGNIIFLNKV AEELSGWTSE DAKGKPSTQV FNIINEKTGQ KCVSPVQRVI
ELGRIIGLAN HTALIAKDGT IRSIADSGAP IRDRESNIIG VVLVFRDTTH EKKLEEELLK
TRKLESLGVL AGGIAHDFNN ILSAILGNIE LAGYRIAKED TRTASLLTDA GKATKRAAKL
TEQLLTFSKG GEPVREIIEL PAFIAESADF VLHGSRIVCN YNFPEDLWRV DVDSGQIGQV
IQNIIINAKH AMPEGGTITI SCTNIEDTAA EALLSVDKGD YVRVTIQDTG VGIPREIIDK
IFDPYFTTKK EGSGLGLAIC HSIINKHDGY LTVHSTIGKG TTFTLYLPAV RSRAGTNSTA
RKTKSTAASK AARIMIMDDE EMLRDVAASQ LAFLGHEAVA VNDGIQAVNR YQELQDNGTP
VDLVIMDLTI PGGMGGQEAA EKLIEIDSNV KIIVASGYSN DPVMANYRKY GFVAAIAKPF
DLKQLSNTIA SILD
//
