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Database: UniProt
Entry: M4S1X1_9SPHN
LinkDB: M4S1X1_9SPHN
Original site: M4S1X1_9SPHN 
ID   M4S1X1_9SPHN            Unreviewed;       548 AA.
AC   M4S1X1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=G432_03685 {ECO:0000313|EMBL:AGH48464.1};
OS   Sphingomonas sp. MM-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH48464.1, ECO:0000313|Proteomes:UP000011816};
RN   [1] {ECO:0000313|EMBL:AGH48464.1, ECO:0000313|Proteomes:UP000011816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MM-1 {ECO:0000313|EMBL:AGH48464.1};
RX   PubMed=23682148;
RA   Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT   "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT   Bacterium Sphingomonas sp. Strain MM-1.";
RL   Genome Announc. 1:E00247-13(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; CP004036; AGH48464.1; -; Genomic_DNA.
DR   RefSeq; WP_015457479.1; NC_020561.1.
DR   AlphaFoldDB; M4S1X1; -.
DR   STRING; 745310.G432_03685; -.
DR   KEGG; sphm:G432_03685; -.
DR   PATRIC; fig|745310.14.peg.756; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_39_5; -.
DR   Proteomes; UP000011816; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
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; 2.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
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; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AGH48464.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011816};
KW   Transferase {ECO:0000313|EMBL:AGH48464.1}.
FT   DOMAIN          13..56
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          317..534
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   548 AA;  58958 MW;  A866767A50885D8A CRC64;
     MATVMTQKNE APPQPDLAAL LDLSHDTIFI RDGATGAISY WNAGAARVYG WEAADLAAPG
     GYGRLQSRCD VPEETVLEEL ARTGHWQGGI TRTARDGSEI IVSARWAARL RPDGSIGEIV
     ETARDVTVKA VAAEELRRSE YRYQNMFRAM AVSFWELDFS GVKGLLREWR DMGVEDFSAF
     FAADPDAVRR VMGATRIVDV NEKTLLLFGA ADRAELGDTV ERFWPRDSEA VFAASVVAAI
     SGKSNFEAET KMLTVDGREV EILFTCSFPP ECMGRGNVLV GVLDISGRVR AQEEVQRVQA
     ELAHAARVAT LGELAASIAH EVNQPLAAIV NFGEAAKRWL NRPEPDMAEA AAAIERMIGD
     SRRASDIIGR IRAMATKSVP KPTLFHPCEA VKEAVQLVRH DMQARGVALS IAEVEAVPRV
     RADRIQIQQV AVNLIVNAVQ AMAQVPEDRR ALVIRTGLAG DNMVRIEVQD SGPGIDPVVA
     DRLFTAFAST KDSGMGMGLS ISRSIVEAHG GTICGRGNEA APGATFSFTL PVAEMTADDA
     AGACTAAA
//
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