ID A0A255YV94_9PROT Unreviewed; 725 AA.
AC A0A255YV94;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=CHU95_17650 {ECO:0000313|EMBL:OYQ32604.1};
OS Niveispirillum lacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Niveispirillum.
OX NCBI_TaxID=1981099 {ECO:0000313|EMBL:OYQ32604.1, ECO:0000313|Proteomes:UP000216998};
RN [1] {ECO:0000313|EMBL:OYQ32604.1, ECO:0000313|Proteomes:UP000216998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH1-14 {ECO:0000313|Proteomes:UP000216998};
RA Cai H.;
RT "Niveispirillum cyanobacteriorum sp. nov., isolated from cyanobacterial
RT aggregates in a eutrophic lake.";
RL Submitted (JUL-2017) 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:OYQ32604.1}.
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DR EMBL; NOXU01000031; OYQ32604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255YV94; -.
DR OrthoDB; 9759607at2; -.
DR Proteomes; UP000216998; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF56; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000216998};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 214..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 471..703
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 703..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 77832 MW; 795F77497F69EF9C CRC64;
MAVERYLGHS GVMRWFWAPL VAALILSLLW AGLSAALTQR PQAVDGVLDL RGWDFRHQGQ
IFLEGDWQFW RDRLVTPGDI ASGKAPAPAL LAVPGRWTNQ TVNGTPLLSE GIGTYHLRVL
LPRNAPPLAM RHNQRFVAWD VLVNGERAIY AGTVGLDADQ TNSAGQKAIA AVSPSDGVLD
ITVQVAAFGG YGGIPRALLL GDADGMYADW HQELALRAAF LSICLSIGLL YLILYVLRPR
DRECLVFSVM SVAIALVQLT SNTPLGSEVL YSLPGQLLGF LNNVMFPVVW LSCLASAALL
FPGSLRKGLA WPSVLFIVAV PVASLWTLQI PWLLTWTATI GLILAMITLI TATVTAARQR
QPLALPMAIA WAVLGVSNLA LVHRVGFTGI MEAGYCFMLF LQAALLIDRL RLMLDQAKQS
NARLAALNGA LEVQVADRTR HLSETVDRLQ LAQDRLVQSE KLASLGRLVA GVAHEVNTPV
GTALTTATHL AQQVAAAEEA MSAGTMTRRQ LADFLTEVKE AACLLTSTVE RTAAVVQSFK
QIATERSDES LRRLDLHDML SELRPAMEVR TDAPHVTLTV ESRPGLVLET NGGALTQVLG
QLLSNCMDHA FPKGRPGHIR VEANLTPAGQ IELVVEDDGV GLADAVRHRL FEPFTTTGRA
EGRTGLGLHM VYTLVAGPLA GTVDIADRTG GGTRVTIRLP AAGRLDAPSP APSSLSTSGM
SAIIT
//
