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Database: UniProt
Entry: I4Z5Z7_9BURK
LinkDB: I4Z5Z7_9BURK
Original site: I4Z5Z7_9BURK 
ID   I4Z5Z7_9BURK            Unreviewed;       410 AA.
AC   I4Z5Z7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Histidine kinase {ECO:0000313|EMBL:EIM31639.1};
GN   ORFNames=LepocDRAFT_00003720 {ECO:0000313|EMBL:EIM31639.1};
OS   Leptothrix ochracea L12.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Leptothrix.
OX   NCBI_TaxID=735332 {ECO:0000313|EMBL:EIM31639.1, ECO:0000313|Proteomes:UP000053899};
RN   [1] {ECO:0000313|EMBL:EIM31639.1, ECO:0000313|Proteomes:UP000053899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L12 {ECO:0000313|EMBL:EIM31639.1,
RC   ECO:0000313|Proteomes:UP000053899};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stepanauskas R., Masland D.,
RA   Poulton N., Emerson D., Fleming E., Woyke T.;
RT   "Improved High-Quality Draft sequence of Leptothrix ochracea L12.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; JH660673; EIM31639.1; -; Genomic_DNA.
DR   RefSeq; WP_009453303.1; NZ_JH660673.1.
DR   AlphaFoldDB; I4Z5Z7; -.
DR   HOGENOM; CLU_020473_1_1_4; -.
DR   Proteomes; UP000053899; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EIM31639.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053899};
KW   Transferase {ECO:0000313|EMBL:EIM31639.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        88..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          220..298
FT                   /note="Signal transduction histidine kinase internal
FT                   region"
FT                   /evidence="ECO:0000259|Pfam:PF06580"
FT   DOMAIN          315..402
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF02518"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  44511 MW;  2016AF8C9D9F623F CRC64;
     MPTRDPLLDF PIEPTQPLVH TAPGDVGGES YRHRSGSAQV RASADERSGG GRDGSSSYDA
     RQGKSRSRRL PAMPVIRKVK LAMSAFDVCH VGVVLRAVLF VHGTVTLGLL FTSQDWLAWL
     ANGAVAATMT LPATLAWLIL ACLGRRKLAA QTVGAQWVAA ILLGAICAIY GWGQMVLLDL
     APVVELGWWP PLAVGMALSA ALFLWLRQRA GLQLPAAAAA RLAELQSRIQ PHFLFNALNS
     AIALVRSDPE RAESVMEDLA ELFRAALASS SATQTLGEEL ALAKRYLEIE RVRFGERMKV
     RWELDPAAHS ALLPVLVLQP LVENAVKHGI EPSETGGEIR IRTRARQGQA RIEISNTVPS
     VPGKAGMGVA LRNVRERLIL MHDVSLRFEV SRVGTTSFRI RIGVPLTGRY
//
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