ID A0A1C5HAS6_9ACTN Unreviewed; 1391 AA.
AC A0A1C5HAS6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-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=GA0070614_1034 {ECO:0000313|EMBL:SCG42977.1};
OS Micromonospora coxensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=356852 {ECO:0000313|EMBL:SCG42977.1, ECO:0000313|Proteomes:UP000198215};
RN [1] {ECO:0000313|EMBL:SCG42977.1, ECO:0000313|Proteomes:UP000198215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45161 {ECO:0000313|EMBL:SCG42977.1,
RC ECO:0000313|Proteomes:UP000198215};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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; LT607753; SCG42977.1; -; Genomic_DNA.
DR OrthoDB; 163538at2; -.
DR Proteomes; UP000198215; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd16936; HATPase_RsbW-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17574; REC_OmpR; 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; 2.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
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; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
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; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 382..598
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 642..757
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 773..841
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT MOD_RES 690
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1391 AA; 148543 MW; 2495B8C8FB6C8C2C CRC64;
MGAAGRPDPG DEGREVAAVG TYGSAYDAAA RVFPGDDPTS VAHRHTDWAA TPLGPVTSWP
AELRAAVRTV LPSTIPMLLW WGPELVQIFN DAYTPIMGDK YPAGIGQAAA ECWPDVWDAM
GPLAEGVLAG RGAAHGENTM LYMYRHGYWE ETYWTFSYSP ICDDRGGVAG IFVATSDVTR
RVVGDRRLSL LRDLGELSIA EADTAADAVR AAVAVLARGH ADLPLGQVYL RERFDAPDAD
TAQQDTLTLA ASFGEAPPGR LATAGQLPEV TQVLRTGHPA RITDLGELLP ESHRPDLHPG
TAPVVEAVAL PLLATGRSRP VGVLVLGVSP FLALDEPYRH FMDLVASRVS TALTDVLAYE
AQRRRASALV ELDRAKTEFF TDVSHELRTP LTLIAAPVQE SLADRREPLP PAQRERLELV
HRNVGRLRKL VNDMLDVARI ESGRTDPDRA PTDLAALTTG VAESFAHAMR RAGLTYTVDV
APLPRTAYVD RDMWEKVVVN LLSNALKYTP AGRVEVRLRG DDTHATLAVG DTGVGVPAEE
LPLVFRRFHR AHGAGHTEGT GIGLALVREL VHLHGGDIEV ESVEGAGSTF TVRLPYGTAA
AAAQPPEIGG PAYPREALSW TAARSTAPAP APAPARPAAA PSVLVVEDNA ELRAFLAGLL
APHYRVVTAV DGRDALEQAR ARPPDLVLTD LMMPRLDGVG LLRELRADRR TATVPVIVLS
ARAGEEAAVE GLRAGADDYL AKPFSSEELR ARVRAHLELS RLRNHEATWR AALIDSLQDA
FVVIEPDSTI VEANEAFGRL VGIARLELPL RPPFAWWPED QLEPEQQARI TGALAAAARD
GRGRVTLPAW HADGHRIWVE AVYNCVREPG TARLLYVATL RDVTTEVGAA ARSATLAALA
SRLAGATDIG EVLDAGLREL CGLVGGARGI AVALDGAGAP VVVGAGVEFT EPVRRVLAEL
RPDGEPQLTR DDAGRVTGIG ARIEPGHAEG GIWVELDRPR PLPALDLPLV RQLGGALAQA
LVRARAFQTQ RTVALAMQRA LLGPVELPGG FAVRYEPAVR PLEVGGDWYD VVPLPDDLVG
VVVGDCVGRG LSAATVMGQL RNACRALLLQ AKSPAEVLAA LDDFARLVPG GGNTTVFCAI
VDRALGVLRY SSAGHPPAIL THPDATSELL DRAGSVPLAS VTVSGRPEAE VRLRPGSTLL
LYTDGLVERR RELIDAGIAR AVAILTEGRQ LLEGELADRL VRDLLPDVRD DDVAVLVYRH
REPALFHATL AADPAQLRPT RESLRAWLVG LGVGESDVEA ALIAVDEACA NAIEHGYRFA
PGATVTVRGH LRADRLEVEV ADTGGWREAG AEGSERGRGR LIMARLMDEA VIDGTPRGTV
VRLVKRLSGT A
//
