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Database: UniProt
Entry: A0A3N4M8Q8_9BACT
LinkDB: A0A3N4M8Q8_9BACT
Original site: A0A3N4M8Q8_9BACT 
ID   A0A3N4M8Q8_9BACT        Unreviewed;       628 AA.
AC   A0A3N4M8Q8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Histidine kinase domain-containing protein {ECO:0000259|PROSITE:PS50109};
GN   ORFNames=EG028_27590 {ECO:0000313|EMBL:RPD37916.1};
OS   Chitinophaga barathri.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1647451 {ECO:0000313|EMBL:RPD37916.1, ECO:0000313|Proteomes:UP000279089};
RN   [1] {ECO:0000313|Proteomes:UP000279089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLT18 {ECO:0000313|Proteomes:UP000279089};
RA   Zong Y.;
RT   "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RPD37916.1}.
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DR   EMBL; RMBX01000022; RPD37916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4M8Q8; -.
DR   OrthoDB; 9778366at2; -.
DR   Proteomes; UP000279089; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF37; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE UHPB; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF17874; TPR_MalT; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279089};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..628
FT                   /note="Histidine kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018195759"
FT   TRANSMEM        369..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          139..172
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          436..623
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          331..365
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   628 AA;  71594 MW;  AC271CAC554C4041 CRC64;
     MSKSLLFFIC MLMVSLSCLA QNQESFVGFG KLPVYTPDSL LQQLKHAGDI KEKMLAAQPL
     IAFHATHGTT DSVIFYAQQM VDALNNSTVK SGDKHLYQSA LFQTLAKAYS EQGLQDEALR
     YYLEGIRLAE ILGNTAAINE NKLGIANVYF ARNEYNKAIE AYNDLLKTTQ DEQLIHTAYE
     RLSVIYLEKN DLIRAKQYAE KALLFFRQQH QLKNELQTKL TLGIIAELDQ HTEEAFSIYN
     EVIKNAQAQQ FFDIYINAGQ RLGDLLIKKK EYENAKGLLS MVYANAMQWN DLKAQLKVLN
     SLRTLHASTG DYKNAYALMT QYMGVSREVL NRQNKKEINE LEIKYQTVQK EKEILNKENE
     LQQQKTIKYG LLIGFLVILL PVIGLLYLYY QKLQAQSKLN TAMDEMNQQK ITALLKDKEL
     ALLKASVSGQ EKERKRIAEE LHDSIGGNLA AIKLRLSSQH NVNGLKELML QVDETYHQVR
     DLSHDLIPQK FTNTGFTELI SGYLRQFDIP GNAKISFQAY PREEIDLIGT TLKVEIYKII
     QELITNSQKH SLASKVEIQL TKMDGLVKLL FEDNGRGFSV ETTKHGIGFQ NIRERLKLFD
     GVLSIDSFPS KGTVIDIEIP LKPEWHEA
//
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