ID A0A437LCG9_9BURK Unreviewed; 844 AA.
AC A0A437LCG9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EOD73_16155 {ECO:0000313|EMBL:RVT83088.1};
OS Inhella crocodyli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Inhella.
OX NCBI_TaxID=2499851 {ECO:0000313|EMBL:RVT83088.1, ECO:0000313|Proteomes:UP000288587};
RN [1] {ECO:0000313|EMBL:RVT83088.1, ECO:0000313|Proteomes:UP000288587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP-18 {ECO:0000313|EMBL:RVT83088.1,
RC ECO:0000313|Proteomes:UP000288587};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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 -!- 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:RVT83088.1}.
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DR EMBL; SACM01000005; RVT83088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437LCG9; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000288587; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000288587};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 327..399
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 403..455
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 603..829
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 844 AA; 94206 MW; 3459C5027DA10C72 CRC64;
MPLLANWVQS TQALLRPVLA TYVRWWRRQS PARQDRFATL GPLASVLLFL MAIVLAFWYL
RNEEVERETE AVKRDTEIAQ QQIRLRLIEN QEQLARMARE VVTRQISPQE FATQATAFAR
ERPEVTHITW LSAHRDRRAS VSSTGFQANH LMAPGTGDPS MPMLGNPPDQ AFTLAKERRQ
TSYSGAFRDA IGSLVFQVHV PLVDRNGFGG VLIAEYGVEA LLRYYVPTEV TTRHPVAMVD
DNILLATTEG PADRRLAPRA VISHDVALAP AFNGLMLRGT GYRTSIGLIS NTLFWMVVAL
AVLTVWMLLG TWRHMRRRLH MQNALLAETN FRRAMENSML TGMRALDMES RIAYVNPSFC
AMTGFTEAEL LGCRPPFPFW PRDRLDENQR LLDQEMQGRS PSGGVEVRVM RKDGSIFDAR
MYVSPLVDAK GKQTGWMTSM TNITEAKRVR DQLSASHERF TTVLEGLDAA VSVVSVPAQE
LLFANRSYRL WFGAENAGHL SLAQEPVRPA ELQGDAVDDA SGLPAQELTD APGGTPREVY
VEAVERWFDV RTRYLQWTDG RLAQMLIATD ITQRRAAEQQ AQVQADKAQV TSRLITMGEM
ASSVAHELNQ PLTAITNYCN GMISRVKGDN IAKEDLLAAL EKTSKQAQRA GQVIHRIRAF
VKKSEPQRVP SQAAEIVDDA VELASFELRR RNVQLHVYVA QRLPALSVDP ILIEQVILNL
LKNAAEAIDN AKLPPSRRHV ELRVVPRHMP DQGGTIEFAV TDTGPGLPEE VLSRMFEAFY
STKTDGLGIG LGLCRSIVES HKGRLRAENL YNGELLSGCR FSFTIPVDAK PTDAPAHPLL
APTP
//
