ID A1T0X8_PSYIN Unreviewed; 1278 AA.
AC A1T0X8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Ping_3719 {ECO:0000313|EMBL:ABM05393.1};
OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM05393.1, ECO:0000313|Proteomes:UP000000639};
RN [1] {ECO:0000313|EMBL:ABM05393.1, ECO:0000313|Proteomes:UP000000639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37 {ECO:0000313|EMBL:ABM05393.1,
RC ECO:0000313|Proteomes:UP000000639};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA Richardson P.;
RT "Complete sequence of Psychromonas ingrahamii 37.";
RL Submitted (JAN-2007) 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; CP000510; ABM05393.1; -; Genomic_DNA.
DR RefSeq; WP_011771941.1; NC_008709.1.
DR AlphaFoldDB; A1T0X8; -.
DR STRING; 357804.Ping_3719; -.
DR KEGG; pin:Ping_3719; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG2972; Bacteria.
DR eggNOG; COG5278; Bacteria.
DR HOGENOM; CLU_000445_127_0_6; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000000639; 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 CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABM05393.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000639};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..268
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 578..810
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 891..1004
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1013..1129
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1159..1276
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 485..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 940
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1062
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1209
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1278 AA; 143539 MW; 9DBA413CCE87C423 CRC64;
MKFKQSIASR LVIINLIRAL VAIIVVASML YTTREIIKSN EELDRAHQTL EHTLAMQVSS
KSLLINGYGF LKSGNPEFLQ TFEQERNEFD TDFAILLEGL SIHAEKSKFT LDIALEIKHI
IDTWLVEEVE PQIIAQRMNV DIYSPKPVLL KSFLYGNALL TKVKDKQAEL IAEEKSFLLK
QQKLVQDTLA WAQLVFIGGI LIFMMLGFVL SYFAATGITR RIGKLVEATQ RLAKGDLDVV
VDITSQDEIG LLGEYTNQTI QRLQHLEVVV KATAAEDFAT QVRVLGQQDQ LALSINKMSE
NLKNSAFERK NQTWLKNGIA ELHSKMRSEH ELVSLSQLVI TYLAKYLNAQ VGSCYLAEGK
QLQLVSSYAF KRRNNNDNVF QFGEGLIGQA ALEQQSILYH QLPDDHNDLL INTGISESTP
TDIFVLPLVH ENKVQAVLAL GVSRKYSQIE LEFLESVASG IAITLHVTRT RQQLVDMLEE
SKLQSEELQA QQEELRASNE ELEEQSTMLV KSEESLRNKS EELQQINSEL EERSEELERQ
TAEMTEKNTV IERAKQAVEI QANNLEKASR YKSEFLANMS HELRTPLNSL LILSQSLAKN
SQGNLNEEQQ EDARVIYEGG QSLLALINDI LDLSKVEAGK LDIHFEQFSI NNLLVNLGRQ
FKPVANKKGV ELCFDKEDVL SDDFFSDPQR IEQVLRNLLS NGIKFTHHGT VSLKVIQPGP
SVRFDNPALR GRNTLGFAVS DTGIGISADN QESVFEAFQQ GDGSTSRNYG GTGLGLTISR
ELVKLMGGEI QLQSKEGEGS TFTLYLPLDR RLGLAAKQPL KANTRESKTH QEPLEISVPT
ADNTREEVVE VSTKADLLKS PLSPVPAREK TLQEKNTFAD DRDILKAGEK SVLVIEDDPS
FMRILIDLSR HKGYRGLSAL TGREGLELAA MYQPSAIVLD LGLPDISGRQ VLEQLKQNIN
TRHIPVHILS AEDKNTEVLQ IGAVGFLTKP VSGEDIDSLF CNIEHLLQDS IKRVLLVEDD
NNNRLAVTRL IANKNIEICS VSTGREAQEK LLSELFHCVI LDLSLPDISG FELLNRLRHN
KSITLPPIIV YTGRELSSEE YKELSQYTSS IVIKGANSPE RLLDETTLFL HSVDSSLPHD
QRKIIKMLHN SELVLQGRKI LLVDDDLRNT YALSKVLREY GLEVIMADNG KLALQKLAEE
ENIELVLMDI MMPVMDGYEA MRKIRSQTRF KKLPIIALTA KAMPEDRTKS IEAGANDYCI
KPIDVDKLIA IMKIWLFR
//
