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Database: UniProt
Entry: H6SK47_PARPM
LinkDB: H6SK47_PARPM
Original site: H6SK47_PARPM 
ID   H6SK47_PARPM            Unreviewed;      1080 AA.
AC   H6SK47;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=RSPPHO_01736 {ECO:0000313|EMBL:CCG08362.1};
OS   Pararhodospirillum photometricum DSM 122.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Pararhodospirillum.
OX   NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG08362.1, ECO:0000313|Proteomes:UP000033220};
RN   [1] {ECO:0000313|EMBL:CCG08362.1, ECO:0000313|Proteomes:UP000033220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220};
RA   Duquesne K., Sturgis J.;
RT   "Shotgun genome sequence of Phaeospirillum photometricum DSM 122.";
RL   Submitted (FEB-2012) 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};
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DR   EMBL; HE663493; CCG08362.1; -; Genomic_DNA.
DR   RefSeq; WP_014414998.1; NC_017059.1.
DR   AlphaFoldDB; H6SK47; -.
DR   STRING; 1150469.RSPPHO_01736; -.
DR   KEGG; rpm:RSPPHO_01736; -.
DR   PATRIC; fig|1150469.3.peg.1959; -.
DR   eggNOG; COG3829; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_000445_114_39_5; -.
DR   OrthoDB; 9796100at2; -.
DR   Proteomes; UP000033220; Chromosome.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00130; PAS; 3.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 5.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF12860; PAS_7; 1.
DR   Pfam; PF13426; PAS_9; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 5.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033220};
KW   Transferase {ECO:0000313|EMBL:CCG08362.1}.
FT   DOMAIN          508..552
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          674..709
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          814..1072
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1080 AA;  117778 MW;  9A36193B5FB99B38 CRC64;
     MTNPERFPPT STSPVPLEGL GDVLEELSCI LFRRTLSPEG RLSYPFLSRN TEALLGFAPE
     DISFGGQDGR DIVLPSDGPA LKAALAVSSQ TLSRCHEQFR VVTATGETRW LRGSANPLLL
     PDGTVHWNGI WQDISTWMRA EHDVKNGTVS REGMLVVQAS GVIAWANGEM ARQFHVPAHS
     LKERSLGDLF PEARARKLSP YPCGAAKTPV GLTARRLDGT TFPFVGTITS VVVNEEESFL
     LVGTNALHEQ DPLRDTLASP DVVLDWFWET DAQDHLTFSS EQIGRVLGVK PSALIGHSWF
     EIGLDDEPGF ALVLRTCLEA RVGFADLVFS VGPEGGHDRR TIRLSGQPLF TPDGFYCGYR
     GVGTDITREV RAERRAERAQ QQLTDAIESF SGAIAVYDAQ DRLIICNPAY SDSFDPSHEF
     VYPGQNFETI LRECYSRGIF DLTDIDFDQW IARRLERHRH ANGEGLVVKL ADGRWMLSRE
     CATQEGGVVS IRTDITELKS REQDLDRLRR RYALILDSTG EGIVGLDASG RVHFANGMAG
     SIFGQVPNAM IGCCFQRLIT GVAVSNPCLP ETALPPSPVM VAFRAGLAGQ VSDEIRRGDN
     GQTVPIDFFV APLIEDDAPA GVVLVFRDAT ERLKFEAFRE QQQHALEQQV SARTADLKRE
     ITVRTRVESA LRESRERLKG ITDSLFEGVV VVDAQGQVVF ANPSARQFLE CGEIEGHPLD
     SVLQVRSPLG PLPFALSPFH TVLSEGTTVR DDDAVFQVSE NKRLDVAYAC SPLGEEAPPE
     AAVISFRDIQ SLKKAQRELF QASRLSSVGQ LAAGVAHEIN TPIQYIGDNL RFIEEAIVKL
     FGLIETAQDL IARTTMGTAD PDGLQRAIAT FQTSATRAKL PFLSAEVPVA VSESLDGVEQ
     ISRIVLSMKD FSHPGTSTKT MTDLNRALES TLTVSRNVWK HGAEVVRDFD PALPPVLCHA
     GEINQVFLNL VVNAVHAIEA SGKPLPGTIT ITTRRDGPMA LIRVSDTGTG IPEAIKDRLF
     DPFFTTKGVG KGTGQGLAIC RDVVVGKHGG TMEASGPVGE GATFVVRLPI EGNDENGSWE
//
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