ID A0A0S2HWY5_9BACT Unreviewed; 1052 AA.
AC A0A0S2HWY5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Precursor;
GN Name=evgS_2 {ECO:0000313|EMBL:ALO14579.1};
GN ORFNames=L21SP5_00911 {ECO:0000313|EMBL:ALO14579.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO14579.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO14579.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO14579.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
RL Submitted (NOV-2015) 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};
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DR EMBL; CP013118; ALO14579.1; -; Genomic_DNA.
DR RefSeq; WP_057952114.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2HWY5; -.
DR STRING; 1307839.L21SP5_00911; -.
DR KEGG; blq:L21SP5_00911; -.
DR OrthoDB; 1116352at2; -.
DR Proteomes; UP000064893; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
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 Gene3D; 1.25.40.10; Tetratricopeptide repeat 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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF13424; TPR_12; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SMART; SM00028; TPR; 6.
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 SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000064893};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:ALO14579.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1052
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006599464"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 123..156
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 163..196
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 203..236
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 243..276
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 544..615
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 619..670
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 688..908
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 933..1048
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 983
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1052 AA; 121489 MW; B2FAE7F15ADA2F59 CRC64;
MKRLVRTLFQ ITILFCLSAT TLTGQNIDSL RKVADTVQGR ELLYTYSEIS RYYWKRNPYL
SFEYAEKVQK IVKNFPKDTL LQIEALHTIG DAYWYLNNIP NALEYDLKVL RLQEKIKDSA
GIAKTLNNLG VIYTHQGKYE KALELLERSL AIRKNLGHTF EASSNYNNLG QVYYKLNDLE
MAMDFFQKSI RIREKNNKQE LLISGYNNVA AVHINRNNYA SAIKYLNKAL NIADSLDIKN
QVPTIMLNLG DIFREQNDYK NAINWYLQAY EIASQIKNYD ILLVISKQLS KIYTETGQLE
KALKYSNYAL EAKDSINSKN IHSKLEQLQY TFNTKQTRLE NKALKQQNEL SELRLNKERN
RTNLLIMLAI LALIIISLLI NLYMQRIRHN KQLKKEVEFR TRSLRREINE RKRFQNQTIE
ANLQFSSIFH NSPLGIVALN NDGSIQMANQ AFQDFANTDE EELKTRNLST LFIESEFIQK
LKTSLQGNDT RYEGKLTFKK ADKPIYARAF FNHYTLSEKE VHGVFVTIED ISISVEAQER
IRHSEERFRT LADLLPEMLV ETDLKGNVLY ANKQALEHFE FSESHIRKGL SVFNLFEPDD
KELIKKRFEN FRAKEKTNIN REYDVTTRTG KKLSILASIS VVFKDAEPVG LRGILMDISN
RKKYEQELLK AKEKAEKADG LKGKFLENLS HEIRTPMNGI LGFSELIKHE EMSEKERASY
IDFIINSANQ LLSIIDDVVN ISRIESGDIK IREQEVSVDN FFNDLMIFFH GYLMNRNDQV
SLRLQNKLTS YANHVILAKK EVQHVLSNLI YNAIKFTRKG YIEIGVQKTN DKLEFFVKDT
GIGIEQHEQE RIFERFYQSH TEGQQSYGGT GLGLTIAKAL VELIGGKMKV KSQPGVGSTF
SFTIPYTPVR KEQDSKLNIP EKKAIYPDWS GKKILVVEDD TNNYLFLEQL LKKTNAQIEH
ATDGKEAVNY VKNNSKIDVV LMDIQMPVMD GYEATRKIRE FNKDLPILAQ TANAMVEDKS
KSLDAGCNDY VAKPVNKKVL LNKIGALIEK SQ
//
