ID A0A0S8BR81_9CHLR Unreviewed; 637 AA.
AC A0A0S8BR81;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Fragment;
GN ORFNames=AMJ56_02490 {ECO:0000313|EMBL:KPK13291.1};
OS Anaerolineae bacterium SG8_19.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703386 {ECO:0000313|EMBL:KPK13291.1, ECO:0000313|Proteomes:UP000050892};
RN [1] {ECO:0000313|EMBL:KPK13291.1, ECO:0000313|Proteomes:UP000050892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_19 {ECO:0000313|EMBL:KPK13291.1};
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:KPK13291.1}.
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DR EMBL; LJNN01000015; KPK13291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BR81; -.
DR Proteomes; UP000050892; Unassembled WGS sequence.
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; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; 1.
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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 273..496
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 517..633
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 568
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPK13291.1"
SQ SEQUENCE 637 AA; 70397 MW; 787F425354B09A63 CRC64;
LVHLNRVVPY DSACIFLMAN DHLRAVAGRG FTHPENVLDI VYPADDNLTV QILSTRQPVI
LQDAKNHPSF NRWGDTDYTR GWMGVPLIVR ESAIGILTVD SKILAAFGPA EAELAQAVAN
QAAITIENAR LFSETQRLLI QTGKQAAQLQ QIMDLVPDGI VMLNEKKRIV LSNQAATSYL
AQLADARVGD ILHQLGNIPL DKLLETGTTK TSWHEITAVE PGGIFEVSSR PLDLSNDNPD
WLLILRNVTD ERREEGYLRT QERLATVGQL AAGIAHDFNN IMTVISLYTQ LVLQTPNVSS
KDQQRLNTIQ QQAERASQLI RKILDFSRQS IVDRKPVDLH PFVKDLTRSW RQSLPDNINI
EADVPDGEYL VEADSARLRQ ALTNLAINAR DAMPWGGNLR LCLGYLILSG DQVYPLPDMK
AGQWITLTIS DTGEGITEKD LSRIFEPFYT TKPTGEGTGL GLAQVYGIVK LHDGFINVES
KPGHGTIFSI YLPAFLPPIE DDSSLDIDKA LSGSGETILI VEDDPDSREA LGEILESLNY
KVLTAPNGTE ALSLYEELNG QVDLVLSDMV MPVMDGAALY AELKARDEKI KMIIITGYPL
DREGKELLNR GVVAYIQKPL QIEVITQAIR AALTNSR
//
