ID A0A1I4SFB6_ECTMO Unreviewed; 1816 AA.
AC A0A1I4SFB6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05421721_11615 {ECO:0000313|EMBL:SFM63031.1};
OS Ectothiorhodospira mobilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=195064 {ECO:0000313|EMBL:SFM63031.1, ECO:0000313|Proteomes:UP000199556};
RN [1] {ECO:0000313|EMBL:SFM63031.1, ECO:0000313|Proteomes:UP000199556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4180 {ECO:0000313|EMBL:SFM63031.1,
RC ECO:0000313|Proteomes:UP000199556};
RA de Groot N.N.;
RL Submitted (OCT-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOUO01000016; SFM63031.1; -; Genomic_DNA.
DR STRING; 195064.SAMN05421721_11615; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000199556; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd00088; HPT; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 5.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SFM63031.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000199556};
KW Transferase {ECO:0000313|EMBL:SFM63031.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 665..772
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 825..930
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1009..1113
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1299..1532
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1534..1672
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1693..1809
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 562..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 670..697
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1142..1160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 712
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 872
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1056
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1742
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1816 AA; 194927 MW; E587922B12B570AC CRC64;
MRQEHRDYSA LRWLRQGLEA LLGEARLALE AYLEEGRDPA HLETLRQHLE QARWTLEMVE
LHGAVLLLQE SAALVDALRD GRVTEPEEAA EVLMRAILQL PDYLEHVRTG HGDLPIVLLP
LLNDLRTMRK ADLLSESVLF LPDLERAPLP PDAPSGAAED VRAWARAQRQ HYQLGLLGVL
RGQEPGNALR RMDRVMDGLY RRAREPRLRR LFWIASALTR ALAGGGLEAG AAVKQLLGQL
DRQIRRLIDA GETELAGDVP EDLVRNLLYY VGRARGEDPR VDEVRRAFHL DRLLPAGEDA
DTARETLGAP NPALMGSVSK ALREELAEIK DRLDVFMHTG GRNPEELAPL VERLRGMADT
LSMLGMGEAR ETALKEAGLL EAMAGGEQAA DEQRLMQAAA ELLHVESALD AAVAGPGPQG
QGDTGLPATL AGLAPGESRA VLKALFHAAL EDLQRIKEAV LEATGAGEGG GDPGDIPGCV
EAIRGGLAML ELTRGTALME GIGHALEAVL PRGEGADPGA LADLAEAITA AECYLEALDS
GVGDAQTLLE IGGEALQRLG FPMPGVASPA AAPEEGPGPE QAPSAEDTAA PVPAPEVGTP
SPGAEERVLV TPERLPEEGE GAWPESFDTA GDGESPSEGD GAAPPEAVPD EAPPAAPQTP
WAVLAGETDA DILEVFLEEA DEELERIREQ LPRWLDDPQD SDALTTVRRA YHTLKGSGRL
VGAELLGEFA WVNEDLLNRV LEGSVPADAG VQALAREALE ALPYLVDQIR GGDTPPMDIP
ALMQRARDLA RGGAKAHAAG PAPEAAPPPS PPGAAGETTT AETAQGRLDP VLLDIYRGET
LQHLQVLDAA LAAARDDPGG LRVTPELQRA MHTLNGSART AGVPETAQVC KACEGYLQAC
AEHHPYRVDA PGISALEDLA AHVRAVLAAL EAPGSEVPQA PELEARFRRL QEAAAQEEAE
APVQDEGGAA PEADATPVVE AVAGAAMEPG EPTDSAMENA AAAEAGQPEE APDPELLEIF
LEEASDLLDA MDTSLQSWGE DLDDREVVHA FQRQLHTLKG GARMAALTPI ADLSHALESL
MIALSEGQKR PHKEMLTPVQ AGLDRLTQMV DCARRGAAIP ADPSLVRHLH AIRSGDGEGS
PVPGPAPGPS PEPERPVAPP ADAAPMDAAQ AEAGPEAQST PGVEPSPPPR SAEEVQPAAR
PAPQEMVRVR SDVLDDLVNH AGEVNIYHAR MEQEITGFGF NLGELEQTIA RLRDQLRRLE
METEAQIIHR HQDERQAPQD GGEEEFDPLE LDRYSNIQQY SRALAESVND LASIHELLYN
QLRDAETLLQ QQSRVSTELQ EGLMHTRMVQ FATMVPRLRR VVRQTATELD RRVELEVEGE
DSELDRSVLE RMLPPLEHML RNAIAHGIEP PDQRRAADKP EIGHIRMRIV REGAEVVLQV
TDDGAGIPLE RVREKVARLG LAPDAEVLTD HELMQYILES GFSTAERVNQ ISGRGVGMDV
VNSEIKQLGG VLSIDSTQGR GTTFTVRLPF TLAISQALLV QTGEELYAVP LSSIEGIVRV
RAGELAGMYA GGDPRYTYAG NDYEVKHLGA LLDVAQPRLE VPDAMLPVLL VRSGNARIAL
QVDALMGSRE VVIKSVGPQV AKVKGISGAT ILGDGRVVMI LDIPALVRAG AGVQLAYHAE
GEEAGGAEAG RATVLVVDDS ITIRKVTARL LERHDFHALT AKDGLDALAL LQETVPDLIL
LDIEMPRMDG FELAAHVRND PRLQGVPIIM ITSRSGEKHR RRAEEIGVDR YIGKPYQEAD
LLAHIRALLQ GEGARD
//