ID I4MWG9_9PSED Unreviewed; 797 AA.
AC I4MWG9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PMM47T1_26138 {ECO:0000313|EMBL:EIK93559.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK93559.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK93559.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK93559.1,
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:EIK93559.1}.
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DR EMBL; AJWX01000035; EIK93559.1; -; Genomic_DNA.
DR RefSeq; WP_008374694.1; NZ_AJWX01000035.1.
DR AlphaFoldDB; I4MWG9; -.
DR STRING; 1179778.PMM47T1_26138; -.
DR PATRIC; fig|1179778.3.peg.5183; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000004339; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; 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; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
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:UP000004339};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 425..646
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 672..786
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 721
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 797 AA; 88959 MW; C55C76310F0D96FA CRC64;
MRYLLILLVG WLPLLACAFD FDESTRTLPL GHVMQVYEDT DGSASIEQVT SAAFAEKFHR
QSEAVLNAGY SRSVFWLRVD LRFVPKDPDA VGNWLLELAY PPMDSIELFM ADKQGRFRLT
QATGDELPYS VREIKQNNYV FAVPFPAYQQ QTVYLRIHSE GSVQAPLNLW SYTAYLEDQP
TRLYVLGLIY GVLLGMLVYN LFIYLSVRDR SYLYYILYIA SFGLYQVSVN GAGVQYFWPE
NPWWANAATP FLIGSAAFFG SQFARSFLQT ADHSRWLDRL LMGLMGVGVV TMLLSLTSTY
GLALRLATAL ALVFTVVIFS AGLIAWWRGL RLARYFIIAW TAFLAGGIIN TLMVLGYLPN
VFITMYASQI GSALEVGLLS LALADRINSM REQQARVLLE AGQKLELLNQ QLANSNRLKD
EFLATVTHEL RTPMNGVIGS LELMQTVPMD TELAQYQQTA AGSARDMMRM VDDILILTEL
QAGKLYPRHE PFGVQALLDN LQMQFARVAQ AKHLAFSVET DSDLPERLQG DSKKLILCLG
CLLDNAIKFT RQGSVGLRVR AGVRTADSLV LSFKVSDTGI GFSQLADATL YQRFSQVDGS
MTREYGGLGI GLAICRQLAE LMGGEISHHS EPGRGSWFQL QVQLGLVNDS GIAPPGLRPN
PQSVQRSPHD CTVLLVDDNS INQLVIRGML LKLGYRVRTA DDGITALELL HRERFDAVLL
DCQTPLTDAF ATCRRLRELP GCARLPVLAV VTHRHERERC LDAGMSDCLS RPVRFEDLQA
ALHRWLLVKA QGESADI
//
