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Database: UniProt
Entry: W1DWP2_KLEPN
LinkDB: W1DWP2_KLEPN
Original site: W1DWP2_KLEPN 
ID   W1DWP2_KLEPN            Unreviewed;       696 AA.
AC   W1DWP2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
OS   Klebsiella pneumoniae IS43.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1432552 {ECO:0000313|EMBL:CDL12534.1, ECO:0000313|Proteomes:UP000019183};
RN   [1] {ECO:0000313|EMBL:CDL12534.1, ECO:0000313|Proteomes:UP000019183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IS43 {ECO:0000313|EMBL:CDL12534.1,
RC   ECO:0000313|Proteomes:UP000019183};
RA   Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT   "Antibiotic resistance diversity of beta-lactamase producers in the General
RT   Hospital Vienna.";
RL   Submitted (OCT-2013) 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};
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:CDL12534.1}.
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DR   EMBL; CBWK010000808; CDL12534.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1DWP2; -.
DR   eggNOG; COG3275; Bacteria.
DR   Proteomes; UP000019183; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   CDD; cd17532; REC_LytTR_AlgR-like; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 2.40.50.1020; LytTr DNA-binding domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR007492; LytTR_DNA-bd_dom.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF13185; GAF_2; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   Pfam; PF04397; LytTR; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00850; LytTR; 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; SSF55781; GAF domain-like; 1.
DR   PROSITE; PS50930; HTH_LYTTR; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          460..573
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          594..696
FT                   /note="HTH LytTR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50930"
FT   MOD_RES         511
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   696 AA;  78053 MW;  3A6DA85444EFE87F CRC64;
     MTALSCMVST IVEGLLGGLV HSVLVKRGRP DKVFSPLTAG AITFVAELVQ MMIILLIARP
     FQDALHLVQS IAAPMMVTNT VGAALFMRIL LDKRAMFEKY TSAFSATALK VAASTEGILR
     QGFNEENSMK VAQVLIQELD IGAVAITDRD KLLAFTGIGD DHHLPGKPIS SSYTQRAIET
     GEVVYADGNE VPYRCSIHPH CKLGSTLVIP LRGENQRVIG TIKLYEAKNR LFSSINRTLG
     EGIAQLLSAQ ILAGQYERQK ALLTQSEIKL LHAQVNPHFL FNALNTLKAV IRRDSDQAGQ
     LVQYLSTFFR KNLKRPTEIV TLADEIEHVN AYLQIEKARF QANLQIQMAV PEGLAHHQLP
     AFTLQPIVEN AIKHGTSQHL GVGEITIRAS QDDRWLQLDI EDNAGLYRAN PQASGLGMNL
     VDRRLRARFW RRLRHQRHLR AGALYPCHPT SAPGGECMLR VLIVDDEPLA RENLRILLET
     QRDIEIVGEC GNAVEAIGAV HKLRPDVLFL DIQMPRISGL EMVGMLDPEH RPYIVFLTAF
     DEYAVKAFEE HAFDYLLKPI EAARLEKTLA RLRQERNLQD VSLLDDAQQT LKYIPCTGHS
     RIWLLQMEDV AFVSSRMSGI YVTDREGKEG FTELTLRTLE SRTPLLRCHR QYLVNMAHLQ
     EIRLEENGQA ELLMRAGQTV PVSRRYLKSL KEAIGL
//
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