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Database: UniProt
Entry: A0A1V3NF52_9GAMM
LinkDB: A0A1V3NF52_9GAMM
Original site: A0A1V3NF52_9GAMM 
ID   A0A1V3NF52_9GAMM        Unreviewed;       876 AA.
AC   A0A1V3NF52;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B1C78_10410 {ECO:0000313|EMBL:OOG23690.1};
OS   Thioalkalivibrio denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=108003 {ECO:0000313|EMBL:OOG23690.1, ECO:0000313|Proteomes:UP000189462};
RN   [1] {ECO:0000313|EMBL:OOG23690.1, ECO:0000313|Proteomes:UP000189462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALJD {ECO:0000313|EMBL:OOG23690.1,
RC   ECO:0000313|Proteomes:UP000189462};
RA   Ahn A.-C., Meier-Kolthoff J., Overmars L., Richter M., Woyke T.,
RA   Sorokin D.Y., Muyzer G.;
RT   "Genomic diversity within the haloalkaliphilic genus Thioalkalivibrio.";
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:OOG23690.1}.
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DR   EMBL; MVBK01000059; OOG23690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3NF52; -.
DR   STRING; 108003.B1C78_10410; -.
DR   OrthoDB; 1931120at2; -.
DR   Proteomes; UP000189462; 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   CDD; cd00130; PAS; 1.
DR   CDD; cd18161; REC_hyHK_blue-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; 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; 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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 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; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 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; SSF158472; HAMP domain-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; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000189462};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..876
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012053276"
FT   TRANSMEM        161..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          188..240
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          245..318
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          319..371
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          512..735
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          756..872
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          228..255
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         806
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   876 AA;  97412 MW;  8ED8E0436B135522 CRC64;
     MKLRTLSGTF LTAALAALLL LGAFSVHAWR TFSGHLEDIH TFSELRTEME QFKSAIDYVT
     LIRSDIDVLQ GVGVDARRLA ESIRTLDPVA GAPAILHLNE IAHLSEVLAE AAPDTSLLHA
     DELQRDTLMA LSRQLLVHRS GVTDVLNTLD RAQDESVATA LMALVGTLTA VAMALALLSL
     IGFTLIHRRL RRPLADLQRG LSLFARGDPD THIPIRGNDE LGELARLFNR MVDQRQQYED
     TLKDQEERFR QLAENIDEVF WMSTPDKRSV LYVSPAFERV WGVSCGALYD RPEVWLDAIH
     EEDRARVIEA AGRQAKGTYN EEYRVVRPDG SVRMILDRAF PIHDDRGQVY RIAGVAVDVT
     HMRQMEVDLR ERVKELRTLY RILELTADAT RTTYEVCEEV ANMLPAGFTW PEHAVARVVI
     GSEEWRSPCW ETPTFKIMST IRHDGTDEGF IEVGYTRLPA EAQPQSDPFL PEEQPLLDGV
     AGHLSRMLHT RRMIHTLNQS DRLSAIGQLT GGVAHDFNNL LTVIIGNAEL LQLRMDRDDT
     LRGLVDMIGS AAQRGAELTQ RLLAFSRHQV LEPRIIDANA HLEGITDLLQ RALGEHIEIR
     FVLTPDLWPA MVDPGQLENA LLNLCINARD AMGDGGFLTI ETANAVLDEH YADTHMEVNP
     GEYVLLSVTD TGEGIAPEIL DKVFEPFFTT KGAERGTGLG LSMVHGFVKQ SGGQISIYSE
     PGHGTTVRLY LPRAAHTDMK DAAATTDAGT RRGDEIILLV EDDRLVRRYA QEQLSALGYT
     VLVATNAHEA LGVLHEHLNV DLLFTDVVMP GGMNGRELAD AARALHPDIR VLYTSGYTQN
     AIVHQGRLDT GVLLLAKPYR QADLARKVRE ALDGPR
//
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