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Database: UniProt
Entry: A0A1T2L8V9_9GAMM
LinkDB: A0A1T2L8V9_9GAMM
Original site: A0A1T2L8V9_9GAMM 
ID   A0A1T2L8V9_9GAMM        Unreviewed;       631 AA.
AC   A0A1T2L8V9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BOW53_03615 {ECO:0000313|EMBL:OOZ41472.1};
OS   Solemya pervernicosa gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=642797 {ECO:0000313|EMBL:OOZ41472.1, ECO:0000313|Proteomes:UP000191110};
RN   [1] {ECO:0000313|EMBL:OOZ41472.1, ECO:0000313|Proteomes:UP000191110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sveles-Q1 {ECO:0000313|EMBL:OOZ41472.1};
RA   Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT   "Mixed transmission modes and dynamic genome evolution in an obligate
RT   animal-bacterial symbiosis.";
RL   Submitted (NOV-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:OOZ41472.1}.
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DR   EMBL; MPRL01000009; OOZ41472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T2L8V9; -.
DR   Proteomes; UP000191110; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 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; 1.
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; 1.
DR   PANTHER; PTHR43047:SF5; 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; 1.
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; 1.
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); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000191110}.
FT   DOMAIN          193..245
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          263..479
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          506..623
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          478..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         556
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   631 AA;  70951 MW;  15D7ADBDF43E4619 CRC64;
     MYGITEAIRH HNQIDEILSA VVEIMPMGWQ HPKHTTARIT IDDMVIIDES FQITPWKMSS
     EITIDERSRG RVEIFYTKSF PEIDEGPFLL QERNLLNSIA KTVSEAIERN EAETALADSE
     QRLREAQSMA HIGNWHSNMT TGDLSWSDEV FHIFGREGTT YIPSLRQYHE SIHPDDLQLV
     ESNVQLARES GSYDATHRIV RPDGSVRHVH ELAQASFNAS GEPVSLTGTI QDITDQIEAE
     QALIIARDEA EQANTAKSDF LSRMSHELRT PMNAVLGFAQ LLEYESTLTE EQQSHIHEII
     IAGNHLLALI NEVLDLAKVE SGKLDMEFEP LQLFPLIKEC SALVSTLAEK RQISISINGV
     SDSVVVADRT RLKQALLNLL SNAIKYNSEK GNIIIEVEAL ADRRIRVLVT DNGTGIPADR
     ISELFEPFTR LSADKTYIEG TGIGLTLTRK IIEAMKGSIG VSSNVGVGST FWFDLPQGTP
     EQSERFTRRS KHSDEPQQTI DKGRVNVLYI EDNSANMRLV AQFISKRPQV RLLEAATPSI
     GLELATAHHP DLILLDINMP EMDGYQVLKR LQKSDELRHI PVIAVTADAM PHDIKRGLEA
     GFSDYLTKPL NIEDFFSHHR STNHHQRDQA W
//
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