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Database: UniProt
Entry: A0A2T6FQX7_9GAMM
LinkDB: A0A2T6FQX7_9GAMM
Original site: A0A2T6FQX7_9GAMM 
ID   A0A2T6FQX7_9GAMM        Unreviewed;       668 AA.
AC   A0A2T6FQX7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B0W54_04290 {ECO:0000313|EMBL:PUA30847.1};
OS   Cellvibrio sp. 79.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=1954207 {ECO:0000313|EMBL:PUA30847.1, ECO:0000313|Proteomes:UP000243979};
RN   [1] {ECO:0000313|EMBL:PUA30847.1, ECO:0000313|Proteomes:UP000243979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=79 {ECO:0000313|EMBL:PUA30847.1};
RA   Zhang Y., Xu J., Wang N.;
RT   "Cellvibrio sp. 79 recovered from metagenome.";
RL   Submitted (FEB-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:PUA30847.1}.
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DR   EMBL; MVDH01000001; PUA30847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6FQX7; -.
DR   Proteomes; UP000243979; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:PUA30847.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000243979};
KW   Transferase {ECO:0000313|EMBL:PUA30847.1}.
FT   DOMAIN          100..152
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          233..285
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          303..521
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          549..666
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         599
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   668 AA;  76168 MW;  77BBE79CE3158DB9 CRC64;
     MIEHISFNPS LQTSDDLELL RSTVGRFQRI FNGSGYGFWE WDLLHQHIEW SGGFWMRLGY
     GPEDAKDICD ASKVLTYIHP DDREFAVEAT RLHLRTGRPM DVSYRIKTKS GDYIWTQVRA
     DSMRDENGQV TIMSGVNFDI TEIKKVEAAL RESEARQVRI IQASSDGIWE WYADRGGFHF
     SHRCWELLGY DDLDDVLTEG EDRLKIWRRH IYQQDLAKFD NALIEHMAGR APFDVEYRLI
     STSGEIRWIR GRGRAVFNEK GQPIMMSGSN MDITEVKRAE ERVIQAKEQA EKANRAKSEF
     LSSMSHELRT PLNAILGYTQ LFEYDGNLKS QQIENVREIR KAGEHLLQLI NDVLDLAKIE
     SGNMTVSLEP VLVSRLLDEC FTLVQTQADA RGIRLKVNIA DHINTYVIAD HVRCKQALLN
     LLSNAVKYNR VGGEVEVTLV AQEGLKLRIS VRDTGRGIPL QRQNEVFQPF NRLSAENSNI
     EGSGVGLVIT KQLVEMMQGK LDFSSAENVG TTFWMDFPVA TEWSADTLTS TNRKKDYSPA
     ILNVQRRCRV LYVEDNPTNI RLLQQIFARY PQLDLDIAEE AFLGIYKARS TSPDLIILDI
     NLPGMDGYEV LAVLKNDPST NQIPVVGLSA NAMPYDIERG RNAGFFDYLT KPVDINQLID
     VFNKLLQD
//
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