ID A0A0S7ZKS0_9SPIR Unreviewed; 771 AA.
AC A0A0S7ZKS0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMS17_07875 {ECO:0000313|EMBL:KPJ87681.1};
OS Spirochaetes bacterium DG_61.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1704237 {ECO:0000313|EMBL:KPJ87681.1, ECO:0000313|Proteomes:UP000050987};
RN [1] {ECO:0000313|EMBL:KPJ87681.1, ECO:0000313|Proteomes:UP000050987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_61 {ECO:0000313|EMBL:KPJ87681.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ87681.1}.
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DR EMBL; LJNB01000090; KPJ87681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7ZKS0; -.
DR PATRIC; fig|1704237.3.peg.3832; -.
DR Proteomes; UP000050987; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
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; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; 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; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 2..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 131..173
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 321..370
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 411..624
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 646..762
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 361..402
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 695
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 771 AA; 87990 MW; B99E62A91130B35B CRC64;
MKVIIVEDNP DHQLIIKRKL KGYYSNIKID ATSNVESAQE LLVKGPYDVL LLDYRLKGAN
GIDLVKWIHE KRIETPIIMI TGAGEVEIAV KAIKLGVYDY LCKNAESFDK LPFLIEKVVK
EHALKRKLNE AEFKYRTLVE GMNEAVFLMK SNGQFLYMSS SVERLLGYSD SELRENFLSY
FSEVDRNNFL KNISLVASGM KVDPFVISFP RGDEEHVFIE INASQFAVDG EQKGVIGTIQ
DVTKHVLLQR EIESERKKIV DIFNSMIDWV YVVDEEYNIK FTNKSLAKQI GDPDRDKCFA
ILYRRSKPCP YCKWEGTKKE LTMRWEMRLD DGKTFDVISS PLKNPDGSIY RMIILRDITR
KKEVEKKYRQ MSEETLKANR ELKSAIDQLK QTQEQLIQSE KLAAIGKLVA GVAHELNNPL
FSAMGFAELL VMDSVKNPGQ REKLENILDS IKRARSIVRD LLKFARRENV EKENININDV
VRETLSLRQY EHKVSDIEVV CDLQEDIPMV FGNFVRLQQV VLNILINAEQ AISDAKEKGA
IRVKTGWDKA GERIVTEISD NGMGISPEVM GKIFDPFFTT KEVGKGTGLG LSTSYGIVKD
HNGQLAVRQD EGWTIFIISL PAVREEPVPD QGETGEEVEV PVAGEKILVV DDEPVIVRLL
EDFFKRKGFN VISAISGSDA LKVLNKNDVE LIITDIKMPQ MDGKQFYEEI KERDPKLLER
LIFITGDTLS TETRSFLRGT GAHFLKKPFS FNEIMKLIDK ILKKTAQREL F
//
