ID K0C5Z8_CYCSP Unreviewed; 1140 AA.
AC K0C5Z8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Q91_1093 {ECO:0000313|EMBL:AFT67131.1};
OS Cycloclasticus sp. (strain P1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT67131.1, ECO:0000313|Proteomes:UP000006282};
RN [1] {ECO:0000313|EMBL:AFT67131.1, ECO:0000313|Proteomes:UP000006282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:AFT67131.1,
RC ECO:0000313|Proteomes:UP000006282};
RX PubMed=23144416; DOI=10.1128/JB.01837-12;
RA Lai Q., Li W., Wang B., Yu Z., Shao Z.;
RT "Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus
RT sp. strain P1.";
RL J. Bacteriol. 194:6677-6677(2012).
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; CP003230; AFT67131.1; -; Genomic_DNA.
DR RefSeq; WP_015005903.1; NC_018697.1.
DR AlphaFoldDB; K0C5Z8; -.
DR STRING; 385025.Q91_1093; -.
DR KEGG; cyq:Q91_1093; -.
DR PATRIC; fig|385025.3.peg.1114; -.
DR HOGENOM; CLU_000445_114_15_6; -.
DR Proteomes; UP000006282; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
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; 4.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08448; PAS_4; 2.
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; 3.
DR SMART; SM00091; PAS; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFT67131.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006282};
KW Transferase {ECO:0000313|EMBL:AFT67131.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 249..322
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 327..379
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 380..425
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 508..563
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 582..634
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 635..690
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 773..998
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1020..1134
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1069
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1140 AA; 127507 MW; 277FB31C00C263A4 CRC64;
MRLSTRLSII VFSLGLTITV LNLYAVRHEV LQQQTHTHRI FAETLVRTMA SVVADDVING
DKEQLTQMLQ VAQNYKNNSI EYLYVIDREG HLFAHSYDTD FPKFLNKQIA KYPSTLNGSR
PINLVAQYNI ENRGLIYEYA VALTPSLSGQ MHLGLNQTKI QVAVNTASKK TLFFGMVLSM
LFTLLAWLAT RYVVRPIEQI STTLQNYQPG GSIDFSFKQS DALDIQTLKY SLKEAFNSRD
YYENLLKQRE QDLEVTLSSI GDAVITTDEQ GHVTRMNHVA ETLTGWSIEE AQGQTVKTIF
PIINASTKEP IPNPVEKVLE TGETVYLSNH TTLISKEGDE YQIADSAAAI RDVNNNILGM
VLVFNDVTEQ YELRQAALQA QQQVEKAFND MQTMVAVLDT DFRVTFINNT PLESLSLKAE
DVIGKEFWMN DWFTYNSALQ KTIQSDCIEA FNGRKTLRDI EIMTNNGVLA LQIGFHPIRD
ENNKVTQLVA EGVDVSVRKH LETEMRASMQ HLQLYREQTP LAAIEWSIDF EVVNWNKAAE
LMFGYTLKEV EGRNFSDMIL PESAVIDVDK IWQGLMTNTG GKNSRNENVT KEGKIILCEW
YNNPLINESG QVIGAVSLVR DITQEHASQQ ALMKSEQEQR DILDTLRDGI ITLSETGVIQ
SFNRAAEHLF GVSSVEAIGQ NISILVREKD EGQPEGYSQA NAMCLLAGSR EAVGVYKKNT
TFPMRLTLAE LPVSANGQHR FACSCQDLTE IKSQQAQIQR AQKMDALGKL VGGIAHDYNN
MLGVILGYTS LMEMKFSNVK GLQKYIGNIS QAGERARQLT KRMLAFSKQK STEAEAEAEA
VDVNSLVDDQ KDLINKSLTA MITVHYQLCD SLGLIWIDKS ELEDTLLNLV INAKHAMPDG
GQLTVSTGAV HLSQIEAEML GLTENDYITL SVKDNGCGID KDIVDFIFDP FFTTKGIDGT
GLGLSQVYGF AGRSGGTIKV YSEKGLGSEF TLYFPLYRGE ERNDTGPIEV KPYRQGEGQA
ILVVDDEPAL RKLALEILTL AGYQVLLARN GNEAIEMLAT TKFDLVLSDV IMPQMDGYQL
AKHIKENYPS IKVQLATGFS SNRHSAMKDK SLQNNMMYKP YRTGELLRRV STLIYGNDDD
//
