ID A0A1V9ES69_9BACT Unreviewed; 1261 AA.
AC A0A1V9ES69;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A4H97_29365 {ECO:0000313|EMBL:OQP48997.1};
OS Niastella yeongjuensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=354355 {ECO:0000313|EMBL:OQP48997.1, ECO:0000313|Proteomes:UP000192610};
RN [1] {ECO:0000313|Proteomes:UP000192610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17621 {ECO:0000313|Proteomes:UP000192610};
RA Chen L., Zhuang W., Wang G.;
RL Submitted (APR-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:OQP48997.1}.
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DR EMBL; LVXG01000016; OQP48997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9ES69; -.
DR STRING; 354355.SAMN05660816_04371; -.
DR Proteomes; UP000192610; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000192610};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 776..800
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 955..977
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 979..1031
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1048..1259
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1261 AA; 144974 MW; 7DC5DAD3A01F875B CRC64;
MNHLQQKLFN RYTYTLLAAI GLFTLAYILN RYVTDVTSPR YFARLIQNRI QQKEQDFQKL
AADTALMGSL VDQTYSEATL QKLLDNKKGY GLYIYDETEF DVPPALLFWN TQLIQPVKHL
SEDSMSSRIE RLSNGIYVHT ARILYLRNDR RLIAEALIPV MRKWQYNVET ENLQKEFVDL
KGATRQVDIS NTVTDFPVKN ISGEVLFYLK QNTLFGKPHN TWVILTTILG FFLLFLFLHQ
VADIVSRTYG IWYGISLLAG VVMAMRLIVY GFPNILALRQ FELFDPAIYG SSFILSSLGD
LLINALLLCW VITFINRRIN ISSIRPYRDP WKNWAALIAS VSALVIVTFM FAAILQTMVS
DAKISFNVTN FFSLIATPYS FIGFIVLATL ALSYFFMSQI LLTVAGKMVG DRNYFMFIIV
GAIGLLILTF TSNNSIVELC LYVLPWLFAF MWLMQQRIFA GLNFRLNVSE VLFWLFVFSG
SMSAVIIFEN GKIELEDRRH FAEKLALQSD PMSEHILSFS LTYLDSNFVV QNMDRFRKSQ
TNAFLKDSIV NKNRDVNFKY NLRLFTFDST DAPLFNDEQA SYDTLNTIFQ IQGKKTAIPG
MRYFEQSFDK FGYIYRRDAY RDTTKLGTLF VLADPRRYKY EALTPELFRS NNPLLPEQYS
SVYSYAIYDN NRDLILNFND YAFPTHLANS LIPQSEFERR RNNSFEELWY RPSSDKVVII
ARKSNTFIEA ITLFAYLFST FLFLLAFYQF SSLIIKSRFH WSALRQTLQL SIRSQIHSTI
LMVSLLSFCV IGVATILFFI NRYQRNNQDR LTRAMQIMVN QVQTHINSQH PQDLRDTIFY
EPVFSEGMER LIQEISDVHG MDVNLYDTVG GLRVTSNQDM NIYSSGVLST KMNPLAYYRL
YHLQQIQTVT NEQVGKLDYL SIYSPIRNEL GHAVAFLNIP SYSSQAELKQ EISNFVVTVI
NLIAFIFLIA GGIALLITNR ITQSFTIISQ KMREVNLGKE NEAIEWKRDD EIGVLVREYN
KMVTKLEDSA EALAKSEREG AWRQMARQVA HEIKNPLTPM KLSIQYLQKA IANNQTDVKA
LTTNVAKTLV EQIDHLSKIA SDFSQFANIG NPKNEVFDLH EMLQSLASLY NTGGNLDFKW
SPVEQRVLLF ADRTQLNRLF TNLLQNAVEA CANRDHRVIR MNEHLNGEFI TVSVTDNGEG
IPEQTQSRIF TPNFTTKTSG TGLGLAMSKG IVEQAKGEIW FVTKEGAGTT FYVKIPLLRA
N
//
