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Database: UniProt
Entry: I4N6I1_9PSED
LinkDB: I4N6I1_9PSED
Original site: I4N6I1_9PSED 
ID   I4N6I1_9PSED            Unreviewed;      1162 AA.
AC   I4N6I1;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PMM47T1_08016 {ECO:0000313|EMBL:EIK97071.1};
OS   Pseudomonas sp. M47T1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK97071.1, ECO:0000313|Proteomes:UP000004339};
RN   [1] {ECO:0000313|EMBL:EIK97071.1, ECO:0000313|Proteomes:UP000004339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M47T1 {ECO:0000313|EMBL:EIK97071.1,
RC   ECO:0000313|Proteomes:UP000004339};
RX   PubMed=22887683; DOI=10.1128/JB.01116-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT   Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL   J. Bacteriol. 194:4789-4790(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};
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:EIK97071.1}.
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DR   EMBL; AJWX01000005; EIK97071.1; -; Genomic_DNA.
DR   RefSeq; WP_008367468.1; NZ_AJWX01000005.1.
DR   AlphaFoldDB; I4N6I1; -.
DR   STRING; 1179778.PMM47T1_08016; -.
DR   PATRIC; fig|1179778.3.peg.1598; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG3706; Bacteria.
DR   eggNOG; COG4251; Bacteria.
DR   eggNOG; COG5278; Bacteria.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000004339; Unassembled WGS sequence.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd19410; HK9-like_sensor; 1.
DR   CDD; cd00156; REC; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF13185; GAF_2; 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; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EIK97071.1};
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:UP000004339};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          500..720
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          771..884
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          893..1009
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1039..1156
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          389..490
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         820
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         942
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1089
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1162 AA;  130578 MW;  6D0EF73B69737922 CRC64;
     MSKPSSIDEQ SFRKLLTRNV SLPLGVGLLS GVVFVGIIAY LMNTIDWVEH TDRVINNANE
     VAKLSIDMET GMRGYLLSGK EDYLDPFELA KPRLAAEVPA LKELVADNNT QVDRLTRIMA
     LQKEWLNYSQ TMIDMKRSTG DYSSVVQTGR GKRLTDAIRG EFEDFIAMEH SLRIQRSEDV
     SHTITLSVTL YILFLVLISA ALAFFGRRDM VSLSTTYGEN LDAQRRSSER LEAQAWLRTG
     QTQLAEQVLG QLTLQMLGRN ILQFFSNYLG SVVAAVYVRE EHGSLRRVAS YGFSREQENR
     DQVIINGEGV IGQVAQNGRL VRLDDLPQDY FKFASGLGEG LPHSVLIVPT HNDDGINGVV
     ELGFLRPLTD RDAELLELLA SNIGTSIEAA RYRQRLQEVL AETQQLNEEL QVQQEELKTA
     NEELEEQSRV LKESQAHLET QQAELEQTNE QLAERTDALA EQRDALDAKN LELNRAQVEL
     EERAEELQRS SKYKSEFLAN MSHELRTPLN SSLILAKLLA ENAEENLTGE QVKFAESIYS
     AGNDLLNLIN DILDISKVEA GKLDVRPENT STARLVDGLR TLFEPLAADK NLAFSVELLE
     GAPTMLFTDR QRVEQILKNL LSNALKFTEH GQVTLSVAPQ PDNGIAFHVR DTGIGVASDQ
     QQAIFEAFRQ ADGTTNRRYG GTGLGLSISR DLANLLGGYI SVSSSLGKGS EFTLILPQRY
     EEAEREEVHP APMVLQPAYS APSEPAPVLV PDVVIARFPD DREQGPFQRR CILVIEDEPN
     FARILFDLAH ELNYHCLVAH GADEGFNLAA QFVPDAILLD MRLPDHSGLT VLQRLKELPA
     TRHIPVHVIS VEDRVEAAMH MGAVGYAVKP TTRDELKQVF GRLEAKLTQK LKRILLVEDD
     DLQRESIARL IGDEDIEITA VGLAQEALDL LRDNVYDCMI IDLKLPDMQG NDLLKRMSTE
     EICAFPPVIV YTGRNMTRDE EAELLKYSRS IIIKGARSPE RLLDEVTLFL HKVESQLSQE
     RQKMLKTARS RDKVFEGRKI LVVDDDVRNI FALTSALEHK GAIVEIGRNG REAIDKLNEV
     QDIDLVLMDV MMPEMDGYEA TREIRKDTRW RKLPIIAVTA KAMKDDQERC LQAGANDYLA
     KPIDLDRLFS LIRVWLPQLE RI
//
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