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Database: UniProt
Entry: A4XT30_PSEMY
LinkDB: A4XT30_PSEMY
Original site: A4XT30_PSEMY 
ID   A4XT30_PSEMY            Unreviewed;       445 AA.
AC   A4XT30;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Pmen_1732 {ECO:0000313|EMBL:ABP84496.1};
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP84496.1};
RN   [1] {ECO:0000313|EMBL:ABP84496.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ymp {ECO:0000313|EMBL:ABP84496.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-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; CP000680; ABP84496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4XT30; -.
DR   STRING; 399739.Pmen_1732; -.
DR   KEGG; pmy:Pmen_1732; -.
DR   PATRIC; fig|399739.8.peg.1756; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_89_27_6; -.
DR   OrthoDB; 9804645at2; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.170; Two-component histidine kinase, sensor domain; 1.
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; IPR031930; HK_sensor.
DR   InterPro; IPR038428; HK_sensor_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF16750; HK_sensor; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABP84496.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        157..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          176..231
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          239..445
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   445 AA;  49793 MW;  AE26737AD5B6438B CRC64;
     MSLPGRHSLL WRLAGALALF CLLLVSLYAD VGRLLVQAAS YLPESTRQVL REHAREAEAA
     WREGGSVGVD TFLEQLRERE GIWAAVVDEH KHSLSSMPLD EVEEQRLDFV RRLDFPVGRP
     GSTPTFYVPF SDGQARLVLE LPQRLDPRQY VELWELLLQR LLPALLAVAL AMLLYRLLIA
     PLAMLRRQAA ALSSGDLSAR LGPQVTQRKD ELGELARSFD HMAERLQGTV AFQRQLLRDL
     SHELRTPLAR LRVAGESEQD VEALRQRLAR EVLQMEKLVG DALELVWLDT ERPRLPSEEV
     DVARLWDVLR ENAAFETGWP VERMPCDLPT DCRVIGHLNG LAQALENILR NAIRHSPQGG
     SVRLGGRREA GDWLLWIEDQ GPGIAESELE AIFRPFTRLS AARPGGDGFG LGLAIARSMV
     ETQGGRVWAH NGEPGLRVHI QLPAT
//
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