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Database: UniProt
Entry: T0HB75_9SPHN
LinkDB: T0HB75_9SPHN
Original site: T0HB75_9SPHN 
ID   T0HB75_9SPHN            Unreviewed;       511 AA.
AC   T0HB75;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=L284_19785 {ECO:0000313|EMBL:EQB09368.1};
OS   Novosphingobium lindaniclasticum LE124.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB09368.1, ECO:0000313|Proteomes:UP000015527};
RN   [1] {ECO:0000313|EMBL:EQB09368.1, ECO:0000313|Proteomes:UP000015527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LE124 {ECO:0000313|EMBL:EQB09368.1,
RC   ECO:0000313|Proteomes:UP000015527};
RX   PubMed=24029761;
RA   Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT   "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT   a Hexachlorocyclohexane Dumpsite.";
RL   Genome Announc. 1:e00715-13(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};
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:EQB09368.1}.
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DR   EMBL; ATHL01000133; EQB09368.1; -; Genomic_DNA.
DR   RefSeq; WP_020820520.1; NZ_ATHL01000133.1.
DR   AlphaFoldDB; T0HB75; -.
DR   PATRIC; fig|1096930.3.peg.3890; -.
DR   eggNOG; COG4191; Bacteria.
DR   OrthoDB; 9789238at2; -.
DR   Proteomes; UP000015527; Unassembled WGS sequence.
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; 6.10.250.2580; -; 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; IPR013656; PAS_4.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
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   Pfam; PF08448; PAS_4; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015527}.
FT   DOMAIN          142..212
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          289..504
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   511 AA;  56432 MW;  044B7E747D651C45 CRC64;
     MVDTRRGPDE IASDVARLAP LFLRQAGGHV LTLLDPAGIV LSYNEEGERA ECWPLDRVLG
     QPHDLFYPPD EIAAGRPCAD LAAALHEGTL EREAWRVCEN GAEYLARLTI SALFEGDAHR
     GFACISRDVT DEAAVRASIE TREQHLQSIL ATVPDAMIII DETGAITSFS AAAQRLFGYS
     ETELVGRNVS CLMPQPDRDR HDEYIAHYLQ TGERRIIGLG RVVVGQRRDG STFPMQLSVG
     EAGEDGQRLF TGFIRDLTAK EQDELRLKEL QAELVHVSRL SAMGTMASTL AHELNQPLAA
     VALYLETIRD MLDERDDEPF VSLRSLMDDA AQETLRAGHI VRRLRDFVAR GEVDKSLHEL
     PRVIAEASQL ALVDARERGI RSFFAVDPAA TPVLVDRVQI QQVLVNLMRN AIEAMAECPV
     RDLKVATRLR PDGLIEVTVA DTGPGIADEV REQLFTAFKS TKADGMGLGL SICRTIIEAH
     GGRIWMERPD RGGARFHFTL IHARAEEEHG G
//
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