ID A0A0F7JWJ5_9GAMM Unreviewed; 896 AA.
AC A0A0F7JWJ5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AAY24_00935 {ECO:0000313|EMBL:AKH19145.1};
OS Sedimenticola thiotaurini.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH19145.1, ECO:0000313|Proteomes:UP000034410};
RN [1] {ECO:0000313|EMBL:AKH19145.1, ECO:0000313|Proteomes:UP000034410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH19145.1,
RC ECO:0000313|Proteomes:UP000034410};
RX PubMed=26089430;
RA Flood B.E., Jones D.S., Bailey J.V.;
RT "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL Genome Announc. 3:e00671-15(2015).
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};
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DR EMBL; CP011412; AKH19145.1; -; Genomic_DNA.
DR RefSeq; WP_046858084.1; NZ_CP011412.1.
DR AlphaFoldDB; A0A0F7JWJ5; -.
DR KEGG; seds:AAY24_00935; -.
DR OrthoDB; 9806704at2; -.
DR Proteomes; UP000034410; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 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; IPR007890; CHASE2.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF32; DRUG SENSORY PROTEIN A; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01080; CHASE2; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000034410};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 313..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 539..579
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 668..883
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 512..539
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 896 AA; 99455 MW; 517268F6CAFB31D6 CRC64;
MLRRVASTIL RVGRGPLRFS PEWLLLSLLL TGGILYMVHS QWLWRLDQLL YDAQLDAWSR
PAPDDLVIVA IDSASLVKYG RWPWPRALHG ELIDRLSDAG ASAIFMDILF VEPDDRDPEG
DLRLEQAVAD SGRVFLPVII ERHDGRLSET LPMPALRMQA RGLGHVDIDL DPDGIARRVY
LREGLGSPRW PSISVAVLQA LQPDAVDPLP GSRNPSGTPA DPNTIVRDHH ILLPFAGSPG
HFHRVSYQDV MAGQFSEDTF ANKIVLVGAT APGLGDLLPT PVSGYSRPMS GVEVNANLID
ALRRGITIQS LALNWQIQLD GLFLLLVFLS FPLLKPNVVL PVVTGMAFLT LAICGLLLHL
FQLWYPPTAI LIGLLFGFPL WSWRRMVRTV HYFEQELTRL RAEPRGIGFH PSTTHISRGL
VFLRMLLPLH GWILLDANGT VLRREKWTAP PTAPMLAIPL EPLIQQQRVW IRIPRGDTYW
QLGVVLDGEP VSDSPSLQLL SDYAGQYAIT HLRERRSNIE RVERQVRRVQ SAIADLRAVR
RLLSDILRQM VDGLLVVNLG GEVVMNNEQA VRLLGMSQEA DLSSLDMLTL SERIEMKNGE
GLIPAFRQVL VQGESHSLEG RLVAGNELLI QVSPLTAAGG SFHGAIIILS DITRLKESER
RRTETLNFLS HDLRSPLASM ISMLEIQRSA VGQMDRAEMA ERIEWYAHKA LKLADDFLRL
ARAENADYAE FQPVDLVTVG QNAVDAVYAE AQKKSIRLVR DMEIESAWIK ADGMLLERAL
INLLENALRH SPVGGVVELR VETGEGEVRC LVRDQGPGIA ESDQQRIFAP FQQVRRGEGN
QQKGTGLGLA FVKVVAVKHR GQITVQSAVG SGTQFCLALP FIDDTPVEHE TGAGLA
//
