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Database: UniProt
Entry: A0A0M2RA81_9PROT
LinkDB: A0A0M2RA81_9PROT
Original site: A0A0M2RA81_9PROT 
ID   A0A0M2RA81_9PROT        Unreviewed;       539 AA.
AC   A0A0M2RA81;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-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=WH95_09420 {ECO:0000313|EMBL:KKJ77339.1};
OS   Kiloniella litopenaei.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Kiloniellaceae; Kiloniella.
OX   NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ77339.1, ECO:0000313|Proteomes:UP000034491};
RN   [1] {ECO:0000313|EMBL:KKJ77339.1, ECO:0000313|Proteomes:UP000034491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-1 {ECO:0000313|EMBL:KKJ77339.1,
RC   ECO:0000313|Proteomes:UP000034491};
RA   Shao Z., Wang L., Li X.;
RT   "Genome sequence of Kiloniella sp. P1-1, isolated from the gut microflora
RT   of Pacific white shrimp, Penaeus vannamei.";
RL   Submitted (MAR-2015) 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:KKJ77339.1}.
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DR   EMBL; LANI01000005; KKJ77339.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2RA81; -.
DR   STRING; 1549748.WH95_09420; -.
DR   PATRIC; fig|1549748.8.peg.3908; -.
DR   Proteomes; UP000034491; 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; cd06225; HAMP; 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; IPR025908; Sensor_TM1.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR025919; Stimulus_sens_dom.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13755; Sensor_TM1; 1.
DR   Pfam; PF13756; Stimulus_sens_1; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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, ECO:0000313|EMBL:KKJ77339.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034491};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        235..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          255..310
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          318..538
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   539 AA;  59331 MW;  12DCE0FB19186251 CRC64;
     MAQTVKKHRK GRKRGWRSSL THKILLINSF VLMIPVVGLM HLEQYRLSLI ASELDALSIQ
     GRAFSLSLGS TAVVASQVGS EKLVPELTRS LMRAMLNDIG VRARIFSTSG EMLADSLYLA
     GVGGPVEVGE LPPPGGIGMM DRIIQFYEEI MNWLPGHDDW PLYREAQHQT AEDYTEVLIA
     LNGEPAGMVR TDTTGRLVLS MAVPVQRYRQ VLGALMLSKD AEVVTQAVQD RRRDILAVCG
     LALGVTVLLS LYLAGIIGRP LRRLANAADF VRYGKGREYE IPDFTHRGDE IGDLSGALRA
     MTEALWARMD AIEGFAADVS HEIKNPLTSL RSAVETVARV SDPEQQKKLL AIIMDDVQRL
     DRLISDISDA SRLDSELSRA KMEEVDVGKL LEALVEIQRV DESCPVFETD IKTDDKLCVQ
     GLEGRLGQVL RNLMTNAKTF SPQDGVIRLA AKSENGRVII TVDDDGPGII PGKFEAIFDR
     FYTERPEDEK FGTHSGLGLS ISKQIIDAHN GTIAAENRTG DDGEVLGARF TISLPEEQR
//
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