ID A0A177NL63_9GAMM Unreviewed; 998 AA.
AC A0A177NL63;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A1359_04380 {ECO:0000313|EMBL:OAI18808.1};
OS Methylomonas lenta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=980561 {ECO:0000313|EMBL:OAI18808.1, ECO:0000313|Proteomes:UP000078476};
RN [1] {ECO:0000313|EMBL:OAI18808.1, ECO:0000313|Proteomes:UP000078476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-45370 {ECO:0000313|EMBL:OAI18808.1,
RC ECO:0000313|Proteomes:UP000078476};
RA Ploux O.;
RL Submitted (MAR-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:OAI18808.1}.
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DR EMBL; LUUI01000076; OAI18808.1; -; Genomic_DNA.
DR RefSeq; WP_066978899.1; NZ_LUUI01000076.1.
DR AlphaFoldDB; A0A177NL63; -.
DR STRING; 980561.A1359_04380; -.
DR OrthoDB; 111890at2; -.
DR Proteomes; UP000078476; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
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; IPR038318; KdpD_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 4.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
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:UP000078476};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 48..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..197
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 197..250
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 247..319
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 321..374
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 447..499
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 708..760
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 779..998
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 998 AA; 112789 MW; 8A8FF3E3420CC018 CRC64;
MVNGRFQIQS VFFYFAAQPA WLRYGLALIT VIAATTATLY IPLIGERAAF LLFFFGIAQA
SFWLGLKPGA LTAVLSLIAV NAFVLFPTGI ELHKILILNA GFCFVSAVML VTTSFNRQLA
EALKESRQNL NHAQSVGKIG SWRMNVQHNQ LQWSEQNHRI FGIPPDTPMT YETFLDTVHP
EDRDYVDKMW QAALNGEPYD IEHRIVITGQ VKWVREKATL EFNKKGKLLG GFGITQDITE
RKQVELERQK FVSLADNSQE FISMCDMNFT SFYVNAAGMR LVGLDSLEQA CRTPVQEFFF
PEDQRFIIEE FLPRLPKEQS GNVEIRFRHF KTGAAIWMIY NVFSIKNNQG DQVGFATVSR
DISARKRAEE ALKMSQDQLR LFVDQAPISI AMFDRDMNYV VTSRRWIDDF GRGYPELIGR
NHYDLHTDIP AEWKQIHRKA QAGAFLKNDE DLWIQSDGSQ LWLRWAVYPW TNQEGEIGGI
IISAENITAY HQAEAAVRAS EAFVSNLLNS LPEHVAVLDN HGEVIAVNEP WKRFALENSS
KPKDVCIGAN YLHVCRQASK VGEPYSGKAL AGLEAILAGR QDEFAMEYLC HTSANNRWFL
MNAKRMSHDS EGVVITHLDI TEHKQAQDEL RESEARLALI IEEAKAGCWD WNPLTSELFL
SSESKRQIGF EDNLLNRWEE WESRLHPDDR AMVWATAKNY ISGHQHNYDL EFRLKHKDGS
YRWIHSRGGL LRDQNNRPSR MLGINLDVTD YKMQKEINER RVELEQSFRL HVAVQTAAAI
AHELNQPLTA ICSYADVATH MLQTGNSNPE KLSQIMGNCS QQAQRAGKVI RQLLTLLQKG
ETTSEAMDIN SSVHKAIEIV KADGLLDVFK IEMNLTADLP PVMANALQVQ KVLINLVRNG
LESMQVEGKD AGILTVTTRP FDVDPAMVLV SVCDSGVGVT DTAALKKIFQ PFYTTKTTGL
GMGLAISRAL IEAHGGKLWA EQNADIGISI HFTLPFEK
//