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Database: UniProt
Entry: A4G677_HERAR
LinkDB: A4G677_HERAR
Original site: A4G677_HERAR 
ID   A4G677_HERAR            Unreviewed;       478 AA.
AC   A4G677;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Signal transduction histidine kinase {ECO:0000313|EMBL:CAL62014.1};
GN   OrderedLocusNames=HEAR1862 {ECO:0000313|EMBL:CAL62014.1};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL62014.1, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL62014.1, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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DR   EMBL; CU207211; CAL62014.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4G677; -.
DR   STRING; 204773.HEAR1862; -.
DR   KEGG; har:HEAR1862; -.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_114_0_4; -.
DR   OrthoDB; 9813412at2; -.
DR   Proteomes; UP000006697; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF10; SENSORY TRANSDUCTION HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAL62014.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006697};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          128..204
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
SQ   SEQUENCE   478 AA;  53582 MW;  60B784D2E917C37E CRC64;
     MHAEWLPTIL QGSVSEIYVL KCDTLRFEYV NPAAANNLQY SIAELAEMSP ATIAQNMTHE
     AYEHFFQDMR NGSRNSVAIN TIHTRKDGST YPIEFQLFYL ASGAEPVIIA IGNDVSSRDK
     SDKALRASES RLGAMVSNTP GLVYQFLLHG DGQFSFPYLS EGCEALLGIT AEALHANPTL
     FVELILPEDR QSYQDAMLAS IEQMNNWNWE GRIWIEKWKD VKWINLRAMP RMLDEHCVQW
     EGLMTNITAS RLEQEEIIRS RAQLAELSAH IDIVKEQERT HIAREIHDDL GGNLTAIKMA
     LALLTRRLPR KNVELIEKAD YVESLVDRTI ESVHRIAGNL RPGILDFGLV AAIDWQGREF
     EKQVGIPCQF SSNKTEIDLA LDQATALFRI FQEALTNIAK HAKASLVTVQ LVHTRQYVRL
     EIVDNGRGIQ MTDRNKPKSF GIRGMVERSI AMGGSLSVST APKGGTIVAI NVPLPEIA
//
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