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Database: UniProt
Entry: A0A0F5IZ52_9BACT
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ID   A0A0F5IZ52_9BACT        Unreviewed;       673 AA.
AC   A0A0F5IZ52;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HMPREF1536_03993 {ECO:0000313|EMBL:KKB50457.1};
OS   Parabacteroides gordonii MS-1 = DSM 23371.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1203610 {ECO:0000313|EMBL:KKB50457.1, ECO:0000313|Proteomes:UP000033035};
RN   [1] {ECO:0000313|EMBL:KKB50457.1, ECO:0000313|Proteomes:UP000033035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS-1 {ECO:0000313|EMBL:KKB50457.1,
RC   ECO:0000313|Proteomes:UP000033035};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Sakamoto M.,
RA   Benno Y., Suzuki N., Matsunaga N., Koshihara K., Seki M., Komiya H.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Parabacteroides gordonii DSM 23371.";
RL   Submitted (APR-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   -!- 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:KKB50457.1}.
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DR   EMBL; AQHW01000020; KKB50457.1; -; Genomic_DNA.
DR   RefSeq; WP_028729470.1; NZ_KQ033920.1.
DR   AlphaFoldDB; A0A0F5IZ52; -.
DR   STRING; 1203610.HMPREF1536_03993; -.
DR   PATRIC; fig|1203610.3.peg.4069; -.
DR   HOGENOM; CLU_000445_114_15_10; -.
DR   Proteomes; UP000033035; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
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; IPR011006; CheY-like_superfamily.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
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; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000033035}.
FT   DOMAIN          170..393
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          408..528
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          551..672
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          133..163
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         462
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         603
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   673 AA;  75980 MW;  D573C0C41AD9CF78 CRC64;
     MEKEAQQSGT NIEYSLLMGL MGVSVSKHLL DEHFTLLWAN DFYYDLIGYP KEEYERLFQN
     RPDIYFKEHK EAWNILGQKV YDAIANNTNG YEAIMKMPVK DGSKWVKLTA TFTDQLQNGV
     PISYTVMIDI TDITEQRELQ KKLEQQSKQL KEALDSAEKA NQAKSDFLAR MSHDIRTPMN
     AIIGMTAIAK AHINEQERVL DCMEKIDGSS KLLLSLINEV LDMSKIESGR LILSEDDFNI
     GELLQDLVIM MQPEIKNKQQ TLDIHVKDLK HEYVTGDTQR IKQVLMNILS NAVKYTPEKG
     QITIDINEKE PKDGTGNYEF VFKDSGRGMK PDFLDKIFLP FERADDNEIR NIQGTGLGMA
     ISHKIIKMMG GDIKVESEYG KGSCFTINMP LHYQEFAPIE KIGTDGLEIL VVDDDETACQ
     STCNCLQEIG INSDYVCSGS EAINKVQLRH QERNDYFAVI IDLKMPDMNG LEATRQIRKI
     IGTDIPIIIL SAYDIEEYEA EAKAAKANGF ITKPLYKSKL LKVLQRFLHE GSRSEPVRQF
     KLSDADYSGK RILLVEDNEL NREIAVEIIG STGVSIDTAV NGLDAVNIVS RSPEGFYQMI
     LMDIQMPVMD GYEATRQIRS LKRSDISGMP IIAMTANAFS EDVTNALKAG MNYHLAKPID
     ISALMSVLGK YLQ
//
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