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Database: UniProt
Entry: D4GGV8_PANAM
LinkDB: D4GGV8_PANAM
Original site: D4GGV8_PANAM 
ID   D4GGV8_PANAM            Unreviewed;       355 AA.
AC   D4GGV8;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=pmrB {ECO:0000313|EMBL:ADD77405.1};
GN   OrderedLocusNames=PANA_2238 {ECO:0000313|EMBL:ADD77405.1};
OS   Pantoea ananatis (strain LMG 20103).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD77405.1, ECO:0000313|Proteomes:UP000001702};
RN   [1] {ECO:0000313|EMBL:ADD77405.1, ECO:0000313|Proteomes:UP000001702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD77405.1,
RC   ECO:0000313|Proteomes:UP000001702};
RX   PubMed=20348253; DOI=10.1128/JB.00060-10;
RA   De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA   Coutinho T.A.;
RT   "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT   Eucalyptus blight and dieback.";
RL   J. Bacteriol. 192:2936-2937(2010).
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; CP001875; ADD77405.1; -; Genomic_DNA.
DR   RefSeq; WP_013026114.1; NC_013956.2.
DR   AlphaFoldDB; D4GGV8; -.
DR   STRING; 706191.PANA_2238; -.
DR   GeneID; 57267922; -.
DR   KEGG; pam:PANA_2238; -.
DR   eggNOG; COG0642; Bacteria.
DR   HOGENOM; CLU_000445_89_37_6; -.
DR   Proteomes; UP000001702; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   PANTHER; PTHR45436:SF7; SENSOR PROTEIN BASS; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001702};
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        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          89..141
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          149..355
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   355 AA;  40156 MW;  91912E187D1EF34A CRC64;
     MNPYRSGNTM RFRLMLTIGM IMLFFQLISV AWLWHESKEQ VQFLVEANLL NRNMDKHVDK
     EVREAILSLA LPSLVMISLT LLLCYQAVRW ITRPLYQLQH ELESRSEVNL EPIIFEGSVQ
     EIDAVTQSIN RLVARLTASL ERERLFTADV AHELRTPLAG LRLHLELLQR NQAVDTQPLL
     QRLDQMSGNV SQLLQLTRAG QQFTSGSYQN VEIVEEVILP MEAELSAMLE TREQTLTLEV
     EDMFRVKGDA ILLRMLLRNL VENAHRYSPS GGNITVRIEA TAGLSLIIED EGNGIDESMR
     GELSKAFVRM DTGYGGIGLG LSIVSRIVQL HGGQFLLENR PDRSGCRARV NFATA
//
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