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Database: UniProt
Entry: W2E5X3_9BACL
LinkDB: W2E5X3_9BACL
Original site: W2E5X3_9BACL 
ID   W2E5X3_9BACL            Unreviewed;       606 AA.
AC   W2E5X3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Histidine kinase {ECO:0000313|EMBL:ETK27033.1};
GN   ORFNames=ERIC1_1c04710 {ECO:0000313|EMBL:ETK27033.1};
OS   Paenibacillus larvae subsp. larvae DSM 25719.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=697286 {ECO:0000313|EMBL:ETK27033.1, ECO:0000313|Proteomes:UP000018834};
RN   [1] {ECO:0000313|EMBL:ETK27033.1, ECO:0000313|Proteomes:UP000018834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25719 {ECO:0000313|EMBL:ETK27033.1,
RC   ECO:0000313|Proteomes:UP000018834};
RX   PubMed=24599066;
RA   Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA   Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT   "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT   Mechanisms of Paenibacillus larvae.";
RL   PLoS ONE 9:E90914-E90914(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ETK27033.1}.
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DR   EMBL; ADFW01000001; ETK27033.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2E5X3; -.
DR   PATRIC; fig|697286.3.peg.534; -.
DR   Proteomes; UP000018834; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 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; IPR010559; Sig_transdc_His_kin_internal.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ETK27033.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, 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}.
FT   TRANSMEM        292..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          313..365
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
SQ   SEQUENCE   606 AA;  69807 MW;  41C61552045FA2A8 CRC64;
     MRFFRWLYNQ YIRSTQIRLT SSFLLVLLPL VFVSLYANDR SRQIVLDQTL SQAQNNLDSQ
     AAHMDLTLKN VEELSRMIAL DKTLLQMLDQ AGPELTPQSI IQFTEILNRL WHVTSISQIL
     SEISVYHAKS GTVVSTKNGA KRITLADQKE VYEQLALSSG IGGTYVLPSQ KIMKDTTFRE
     LSGSEMVSLV RTMDLSAWSK HSNLLIVTLN KKKLNELILS ALPSAGTHLY LFEKDGNIIT
     GSDQPDSGTG FINVKKEGML RIQAELPSYK WSLVMLQPEQ EIYGQTGVVR TYTYLIIVIS
     VLLSLILSWW VFIRIASPLD RLSYGMKELS SGNYDLRLDT TRKDEFGYLM KTYNKMARHQ
     KHLIEDYYEQ QLRLANTELK FLQSQINPHF LYNTLDSIYW MAKNYEAEEI SEMVLNLSRF
     FRLSLNKGKE AFTVEETISH LHYYIRVQQI RFLDSFTVSY QIQEESKTIP VYKLLLQPLV
     ENALLHGLER KQEGGELIIS SYLEEEYLVL SVQDNGDGIN RERLDYIQQE LGSLAQNKAA
     ILHDMERTIQ DLYGLRNVLI RLKMMYGPKA DLQLESEEGV ETRITLFIPL DSCKSEFIMD
     GKERLA
//
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