ID A0A1Q6CNS7_9GAMM Unreviewed; 1019 AA.
AC A0A1Q6CNS7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BI291_06140 {ECO:0000313|EMBL:OKY28078.1};
OS Thalassotalea sp. PP2-459.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1742724 {ECO:0000313|EMBL:OKY28078.1, ECO:0000313|Proteomes:UP000186791};
RN [1] {ECO:0000313|EMBL:OKY28078.1, ECO:0000313|Proteomes:UP000186791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP2-459 {ECO:0000313|EMBL:OKY28078.1,
RC ECO:0000313|Proteomes:UP000186791};
RA Barja J.L., Dubert J.;
RT "Draft genome of the tyrosinase inhibitors producing Thalassotalea sp. PP2-
RT 459.";
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 -!- 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:OKY28078.1}.
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DR EMBL; MKQD01000003; OKY28078.1; -; Genomic_DNA.
DR RefSeq; WP_074495152.1; NZ_MKQD01000003.1.
DR AlphaFoldDB; A0A1Q6CNS7; -.
DR STRING; 1742724.BI291_06140; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000186791; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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 Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000186791};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 315..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 350..395
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 512..732
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 888..1011
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 850..877
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 941
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1019 AA; 114593 MW; E9E658A4815335E5 CRC64;
MNKKWKFYLG ASLLLCVIIV ASGFIYNNTA SIEARSINEI NQVHENIMEE LNSEFSSLSN
EVSFLHFTPP VRGLARANKN NDIDVLDGST TELWRKRLEQ IFIGFLKNYD EYFQLRIILN
NGDEFLKVIR QKGNISSVPA NVLQNKAHHD YFTEAVNSPT KNMLFSRISL NKENNTIEIP
HVPTLRLSIP IYQDEGTLYG VLVANVDVTK IFNSVRGLIT DHQQLMVMDD EGYYLCHEDG
TLKYSRDLSP EHRLNQDYIF ENEEADALSI SSSTSKEQFR GILKQLQLPV DGKGNTLQVA
LMLPQKYINA QKTQALTSSI IVLFIVVIIA LSILVYFYNL SNKASRLAKQ FESGQRIIDS
TNEAVFVLNK QHSIISCNTA ASNLMRASVN ELVGKAISSV LKEHLTLDIT SIFTHFSAST
PINHQTLKAT QGNTTLYLNC KAIPLFRDTV KKKTPKLALL ISDVTAENEA YNLIEQQKFN
LEKEVELRTS ELEIARDKAV ELSDIKSRFI STISHEMRTP LNGITGAIQL LKRDIHSQDE
NDYISMAENG IETLSSLVND ILDISKIEAG KLELNYQHHQ IHDVIESLVS TLSIVIKEKG
LTFYIDTSHL TIASAKFDAF RLKQIISNLV SNAAKFTKEG YIKITAESIT TESTVILNLT
VEDTGIGISE DELTHLFQEF SQANRTITEE YGGTGLGLSI CKQIANLMGG DIHVSSQLGK
GSTFTVTIML EECVSFDAQV KTRLQGKYFC VCIEDPIECS IIERLINFSG GSLIPITSNI
TQLLLENTID YLVTDTSFLK ADNNIADIKK ALKDNTLTRW LIIDNGRYDL SKISSQATVI
ESPVLRADFL ESVLHERNRE EQKINDTRRK YDKEQLLNQQ QLISSPVHVL VVDDNRINRK
VAQHMLEGMG LTVSTAIHGE DAIEQLQNSN DESQFSIIYM DCNMPILNGY DTTTLIRQGN
AGKRYQTIPI MAMTANAMKG EQEKCQAAGM NDYITKPVNV NILEQKTYQL LEKTHKKTD
//
