ID A9AUH6_HERA2 Unreviewed; 713 AA.
AC A9AUH6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Haur_0444 {ECO:0000313|EMBL:ABX03095.1};
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC Herpetosiphonaceae; Herpetosiphon.
OX NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX03095.1, ECO:0000313|Proteomes:UP000000787};
RN [1] {ECO:0000313|Proteomes:UP000000787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95
RC {ECO:0000313|Proteomes:UP000000787};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABX03095.1, ECO:0000313|Proteomes:UP000000787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95
RC {ECO:0000313|Proteomes:UP000000787};
RX PubMed=22675585; DOI=10.4056/sigs.2194987;
RA Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A.,
RA Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H.,
RA Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C.,
RA Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA Goker M., Woyke T., Klenk H.P., Bryant D.A.;
RT "Complete genome sequence of the filamentous gliding predatory bacterium
RT Herpetosiphon aurantiacus type strain (114-95(T)).";
RL Stand. Genomic Sci. 5:356-370(2011).
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; CP000875; ABX03095.1; -; Genomic_DNA.
DR AlphaFoldDB; A9AUH6; -.
DR STRING; 316274.Haur_0444; -.
DR KEGG; hau:Haur_0444; -.
DR eggNOG; COG2204; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_0; -.
DR InParanoid; A9AUH6; -.
DR BioCyc; HAUR316274:GHYA-450-MONOMER; -.
DR Proteomes; UP000000787; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABX03095.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ABX03095.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 351..574
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 594..711
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 646
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 713 AA; 80670 MW; 48593F3E436CC531 CRC64;
MKRFAWLRRK ELRPLIALLS VALVSIALLQ WNYYQMRSMI QSQITAFNGM TQARLNMKRG
YLIAEQVLNG NQTLLPQDAI AYLDQAILAV DDWQQGKNPV VVFDQLLPPD PPTQQALTDY
RQHLVSFRAL LLQHLNRPQE QAQTTIDRRI AFSELESEAE QLENRLYLDL ELSIKRQAER
YSLMLVGWLI FLVIIAGVVY RLLGLQRLAV AQLAASEKQF RAQYRGIPIP TYTWRCIDDD
FILEGFNDAA MIITQGAITK FVNQSARIVY RNEPEILHHF ERCQREKITL HQEIRYEFKL
INQVKDLYVS YVFIEPDFIM VHTEDRTDRN QLQMQLIRAQ KMESIGRLAG GVAHDFNNLL
TAISGYTTLA IDSAQQGFPV VEELTEIQHA TDRAAMLTSQ LLTFARKQQI QPKIVNINDL
IMSMEKLIRR VLPESIQWRT VLNVNIDLVL ADIGQIEQVL LNLVVNARDA MPQGGNLLVE
TNNVAVDANY ARTHIDVPIG NYVLFAVSDT GIGMTQEVQS RAFEPFFTTK SDHEGTGLGL
ATCYGIIKQH GGHIGLYSEV NHGTTIKIYL PRSEQAQLDD APSLIQNLPR GTETILVSED
EPQVRAVLVR MLQGLGYSVL EALHGSEALA LLQAQALGTI QLLITDMVMP QMGGFELSQR
VAELDPQLKI LFISGYSEHS LAQHQQLAQQ PLLLSKPFSL ATLAQTVRKV LDD
//
