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Database: UniProt
Entry: A0A1I4SFB6_ECTMO
LinkDB: A0A1I4SFB6_ECTMO
Original site: A0A1I4SFB6_ECTMO 
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};
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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
//
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