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
//