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Database: UniProt
Entry: Q1N822_SPHSS
LinkDB: Q1N822_SPHSS
Original site: Q1N822_SPHSS 
ID   Q1N822_SPHSS            Unreviewed;       653 AA.
AC   Q1N822;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   08-NOV-2023, entry version 90.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SKA58_11483 {ECO:0000313|EMBL:EAT07139.1};
OS   Sphingomonas sp. (strain SKA58).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=314266 {ECO:0000313|EMBL:EAT07139.1, ECO:0000313|Proteomes:UP000005395};
RN   [1] {ECO:0000313|EMBL:EAT07139.1, ECO:0000313|Proteomes:UP000005395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKA58 {ECO:0000313|EMBL:EAT07139.1,
RC   ECO:0000313|Proteomes:UP000005395};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (MAR-2006) 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:EAT07139.1}.
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DR   EMBL; AAQG01000025; EAT07139.1; -; Genomic_DNA.
DR   RefSeq; WP_009822054.1; NZ_CH959306.1.
DR   AlphaFoldDB; Q1N822; -.
DR   STRING; 314266.SKA58_11483; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_51_5; -.
DR   OrthoDB; 9796100at2; -.
DR   Proteomes; UP000005395; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 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; 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; 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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 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; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EAT07139.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000005395};
KW   Transferase {ECO:0000313|EMBL:EAT07139.1}.
FT   DOMAIN          9..66
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          84..136
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          137..192
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          212..264
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          284..504
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          526..635
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         575
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   653 AA;  70780 MW;  0216351FCF0F2146 CRC64;
     MNTLPSEYSG NRFELLVQSV TDYAIFMLDT DGRIASWNAG ARRFKGYEPD EIIGQHFSRF
     YTPQDQAAGI PAAALATAQQ EGRFEAEGWR VRKDGTHFWA NVVIDPIRDT DGRLLGFAKV
     TRDLTERRAA DEALRKSEER FRLLVESVSD YAIYMLDPVG TITSWNMGAE RAKGYKTDEI
     LGKNFALFYS EDDRIAGLPS RALHSAERDG RFESEGWRIR KDGSRFWANA VIDAIRDSAG
     QLIGFAKVTR DLTERRESQL ALEDARAAIM QAQKMDAIGK LTGGVAHDFN NLLAVIVGSL
     ELARMRLAKG GDIERFLDNA MAAADRGATL TQRMLAFARR QELKLQSVDC LALVHGMTDM
     LQSSVGPGII IDSLFPKSLA PAHADTGQLE MALLNLVVNA RDAMPDGGRI LISASEMLTA
     QGTVPGLASG TYVKLSVIDE GQGMDSATLE QAREPFFTTK GVGKGTGLGL SMVHGFVEQC
     GGALTIESTV GAGTTVSLWL PVSQEEETSI VGTDTPEGPL MQTPLVILAV DDDDLVLTNT
     AGMLEDLGHT VFRAGSAADA LRMLEQSRID MVVTDHAMPG MTGAQLADAI EEAHPHLPVI
     IITGFAELPA HSSSRPRLDK PFRQAQLARL VNQVGALSSG KERISFGPST DPL
//
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