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Database: UniProt
Entry: A0A220W3X3_9SPHN
LinkDB: A0A220W3X3_9SPHN
Original site: A0A220W3X3_9SPHN 
ID   A0A220W3X3_9SPHN        Unreviewed;       358 AA.
AC   A0A220W3X3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SPHFLASMR4Y_00748 {ECO:0000313|EMBL:ASK87530.1};
OS   Sphingorhabdus sp. SMR4y.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=2584094 {ECO:0000313|EMBL:ASK87530.1, ECO:0000313|Proteomes:UP000198359};
RN   [1] {ECO:0000313|EMBL:ASK87530.1, ECO:0000313|Proteomes:UP000198359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMR4y {ECO:0000313|EMBL:ASK87530.1,
RC   ECO:0000313|Proteomes:UP000198359};
RA   Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA   Clarke A.K.;
RT   "Genome Sequence of Sphingorhabdus flavimaris Strain SMR4y Isolated from a
RT   culture of the Diatom Skeletonema marinoi.";
RL   Submitted (JUL-2017) 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; CP022336; ASK87530.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A220W3X3; -.
DR   KEGG; sfla:SPHFLASMR4Y_00748; -.
DR   OrthoDB; 9760752at2; -.
DR   Proteomes; UP000198359; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00130; PAS; 1.
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; IPR036890; HATPase_C_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR   PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR   Pfam; PF07536; HWE_HK; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   SMART; SM00911; HWE_HK; 1.
DR   SMART; SM00086; PAC; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50113; PAC; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ASK87530.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198359};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ASK87530.1};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          107..159
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
SQ   SEQUENCE   358 AA;  40334 MW;  FED05624CE3E0346 CRC64;
     MPTRSQIKNF RLNEYRDRHT NDVRLQERGA LQQSGDAFHA LADTMPQMVW STLPDGDHDY
     YNARWYEYTG APDGSTDGEA WAEMFHPDDQ PEAWKRWNHS LETGEPYEVE YRLRHRSGQY
     RWVLGRALPI IGPDQKIQRW IGTCTDIEDA KQTASHNEML SQELSHRIKN IFAIISGLIS
     MTARGDASFR EPAETLKGRI AALGRAHEYV RPHNDRDQSV LGDVTMQRLL SEIFASYPAF
     SDNRLQISGG DIAVGDRAAT PIALVFHELA TNSMKYGALA ADEGQVELEI SRDQDMVLFK
     WSEHGGTPIE SPPTGSGFGS KLVEMSVTQQ LGGKLERFWL PAGLRIEMQV QASRLSGS
//
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