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Database: UniProt
Entry: Q6LMX1_PHOPR
LinkDB: Q6LMX1_PHOPR
Original site: Q6LMX1_PHOPR 
ID   Q6LMX1_PHOPR            Unreviewed;       572 AA.
AC   Q6LMX1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=Z3303 {ECO:0000313|EMBL:CAG21355.1};
GN   OrderedLocusNames=PBPRA3027 {ECO:0000313|EMBL:CAG21355.1};
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG21355.1, ECO:0000313|Proteomes:UP000000593};
RN   [1] {ECO:0000313|Proteomes:UP000000593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CR378672; CAG21355.1; -; Genomic_DNA.
DR   RefSeq; WP_011219617.1; NC_006370.1.
DR   AlphaFoldDB; Q6LMX1; -.
DR   STRING; 298386.PBPRA3027; -.
DR   KEGG; ppr:PBPRA3027; -.
DR   eggNOG; COG3275; Bacteria.
DR   HOGENOM; CLU_020473_3_3_6; -.
DR   Proteomes; UP000000593; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   PANTHER; PTHR34220:SF10; SENSOR HISTIDINE KINASE BTSS; 1.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        42..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        71..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        138..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          224..362
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   572 AA;  63501 MW;  1F051ED9581A7097 CRC64;
     MELIFSLLQQ LSVYLVIAYL LSKTPLFMPL TTVSGRLSQR FSCYVLFSLF CILGTYFGLN
     IEDAIANTRA IGAVMGGLLG GPIVGFAVGL TGGMHRYSMG GFTDVACAIS TTTEGLLGGL
     LHSYYVRRGQ VDQLYRPFIV FTITLVAEII QMFIILIVAE PYDKALHLVS AIALPMVIAN
     SLGAALFMSI IQDRKTIYEK YSAAFSSRAL KIAQRSVGIL SQGFNEESTK KIAKIVYEET
     GVGAVAITDR DKILAFIGIG DDHHLPGTPI SSGYTRRSID NCELVYADGH DMPYCCSLSN
     RCKLGSALVI PLVGGNNDVL GTIKLYEPKR KLFSTVNLTL GEGIAKLLSN QILTGRYEQQ
     QILLTQAELR LLQAQVNPHF LFNALNTISA IIRRDPDKAR QLIQHLSQFF RRNLKQNIET
     VTISEELQHV RSYLEIELAR FSDRLNVEII VPDELMSINL PTFTLQPLVE NAIKHGTSSL
     LENGQIIIRG YVFDNHLVLE VEDNAGTYQP VSEESGLGMK IVDKRLKNMF GQQYGLKMSS
     QPNIWTRATI TLPEDKTLQH NDINKTYTAE NK
//
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