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Database: UniProt
Entry: A0A162QAA9_9BACT
LinkDB: A0A162QAA9_9BACT
Original site: A0A162QAA9_9BACT 
ID   A0A162QAA9_9BACT        Unreviewed;      1139 AA.
AC   A0A162QAA9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A1D16_11070 {ECO:0000313|EMBL:KYP15292.1};
OS   Flavihumibacter sp. CACIAM 22H1.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavihumibacter.
OX   NCBI_TaxID=1812911 {ECO:0000313|EMBL:KYP15292.1, ECO:0000313|Proteomes:UP000075747};
RN   [1] {ECO:0000313|EMBL:KYP15292.1, ECO:0000313|Proteomes:UP000075747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CACIAM 22H1 {ECO:0000313|EMBL:KYP15292.1};
RA   Moraes P.G., Lima A.R.;
RT   "Draft Genome of Flavihumibacter sp. CACIAM 22H1.";
RL   Submitted (MAR-2016) 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:KYP15292.1}.
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DR   EMBL; LUKG01000019; KYP15292.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162QAA9; -.
DR   STRING; 1812911.A1D16_11070; -.
DR   Proteomes; UP000075747; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 5.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 5.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 5.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 5.
DR   SMART; SM00091; PAS; 5.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          114..179
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          530..600
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          721..772
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          850..902
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          927..1139
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          893..920
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1139 AA;  130407 MW;  4053E93F7626E652 CRC64;
     MAMVDFLLNE IPYPAVVLRI ADDEPVCITH SNKAFQETDQ LGTTICASPA LNHWVKKIKL
     HKNTAPVQSL QKDKLVIDGP FSSKLLLELS LLPGSGTAER QLLCTIPPVH QPTPGNSYSS
     LIAGTTDLCV ILNKAGEYTY LSANFPAMLG YDAAELMGTN SLELVHPDDI SATRQAFERL
     GSELSVQAPP FRYRKKDGSW CWLQSVGTNL LELPSVQGFV INSIDITQLV EAHQLLKQNN
     ERYQLIYKAS NDALYDWDIE ADSFYWGEGF YRLFGHSAKT TPFRLANWIE LTHYQDAEKN
     KQRWDEFLKD TQQNSWINKF RFRKADGSYA YVEEIAYLIR DKEGRPLRMI GSIRDKTESK
     LVLLRKLIEQ DITDLFKSTD TLPAILQRVT DYLAQTGNWS LAELWLLNNR QDKIKLVAYH
     LNPQTEKAFY PGSQPVQEFS PGNGLPGTVW KNKQPTYWDQ TSIQKNFIRK EAASKANLKA
     ISGLPIFDNG QILGTLVLGK NTDLEEQQAN LEILESILPS LGTEIRRKQQ EEEMRLVFES
     APDILAIVSP EGYFTRVNPT FCAIMGYSSQ ELTSRPYHMF IHPDDVMQTL KEFGEIIPLN
     KKAVNVVNRY ITKTGEQRWI SWSSSEIFGS EKLAFAYGRD ITEMKELEDL IDNTSKLARV
     GSWEINMSDK YIFCSKITRQ ILELKDGLQL RLNNRLEYIR HSSRERVRKL LQEVLFDQKP
     WDIEVEIRTA KGASRWVRLI GQASFHQGRC VRIYGSIQDI HEKKLVQLQL EEANDRFERV
     SSATNDAIWD WDLIHNRLIW NDRFSKIFGY PVKAEGTGPN EWKDMVHPDD LPLLGKNIRE
     ATNDPEHHHI DIEFRFRRSD GSYAYVSNKG TLIRNKEGQV IRMVGALSDI SVRKNFESSL
     KNLNQELKRI NHELAGSNAE LEQFAFVASH DLQEPLRMIT GFLTMLEKKY GPQLDEKANQ
     YIYFAVDGAK RMRGIILDLL EYSRVGRMNT TRELVDANLV IKDVVQLLQN QLEEKNVGLS
     VHPMPSLYTY KLPLQQVLQN LISNAIKYSQ PGKQPLIEVS CQELDQYWEF SVKDNGIGIE
     AAFKEKVFVI FQRLNYTPEI PGSGMGLAIA KKIIDWQGGE IWVESVVGEG SIFYFRLPK
//
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