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Database: UniProt
Entry: H9UH18_SPIAZ
LinkDB: H9UH18_SPIAZ
Original site: H9UH18_SPIAZ 
ID   H9UH18_SPIAZ            Unreviewed;       883 AA.
AC   H9UH18;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Spiaf_0711 {ECO:0000313|EMBL:AFG36811.1};
OS   Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG36811.1, ECO:0000313|Proteomes:UP000007383};
RN   [1] {ECO:0000313|Proteomes:UP000007383}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC   {ECO:0000313|Proteomes:UP000007383};
RX   PubMed=23991249; DOI=10.4056/sigs.3607108;
RA   Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA   Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA   Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT   type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT   Rift.";
RL   Stand. Genomic Sci. 8:165-176(2013).
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; CP003282; AFG36811.1; -; Genomic_DNA.
DR   AlphaFoldDB; H9UH18; -.
DR   STRING; 889378.Spiaf_0711; -.
DR   KEGG; sfc:Spiaf_0711; -.
DR   PATRIC; fig|889378.3.peg.722; -.
DR   eggNOG; COG2984; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_20_12; -.
DR   Proteomes; UP000007383; 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   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007383};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          360..406
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          431..485
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          503..759
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          650..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   883 AA;  98578 MW;  F7B6690C52F5DBBF CRC64;
     MLLLISVALS GAAEAQPRIL ALHSYHTEYL WTARQIRGLE NALDELLGPT QLFHEFMDAK
     RIDPLGYEPD LLNLLRNKYR NITFDLVFVS DEQAYDLYSR HGQQLFPDTP MVFAAVDTID
     PRFDRRRPPH TGIYEAVELA PIVRLMQRLH PDTEKFLVLS DDRPGLPGFL NQIEAGRRGW
     DAEPIILIAP ERQELDTVLQ KHPKIPMLFL GYFSPPDGIS LSLSESVQLI LNAGRRPIYT
     AWDDALDTGV LGGYMTSGYQ HGYAAGEYIA KILADGVAPW ELPIRREGIN RYLIDYPVMR
     ELGLQPGSFP PGTIFHNSPE ELFARYRRYL VITIAVIAVL SLMILLLLVN NGRRRIAERH
     TRAFRRAVES TAHAVYLTDP AGIITYVNPA FEQLTGYSRS EVVGQNPRLL QSGRMPRDYY
     TRLWATIQVG SQWYEQITNQ RKDGQLYTAD QTISPLIGTK GQLEGYVAVQ IDASERLAVQ
     DALLQAKMAA EDSDRAKTAF LRTISHELRT PLNGILGFSR LILEQQTDDQ TSDYAKHIVE
     AGTQLNSIIT SIIDLSRIES RSIGLETDRV NPVGIVRELV ALYQPRTRDT AIRILDNPAG
     SSVPNVYMDP VRFRQLVDIL LDNAVKFTPS GEISIKLRWC SRANSVKPAD AARAKTATQP
     TGSPQPEAAA TDEDPARGPQ TGTLAVRIRD TGIGLDPAEI DRIFQPFYQA DSSDARRFGG
     SGLGLTIAQR LCTQMGGRLE AHGTPGEGAV FTLLLEGIQP ASQRTDTHNP HQAAADSEPA
     SRSFPDALTA ETWLNREIEN FATLKARMIP RDLQSWAQQQ VASGILSDPD SRLGQLLRKL
     ADAAENWDVQ RMPRYMADID SFMRELSGED TRNAHHTGEE TSE
//
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