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Database: UniProt
Entry: A0A1M6M444_9FLAO
LinkDB: A0A1M6M444_9FLAO
Original site: A0A1M6M444_9FLAO 
ID   A0A1M6M444_9FLAO        Unreviewed;      1260 AA.
AC   A0A1M6M444;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04488007_1414 {ECO:0000313|EMBL:SHJ78229.1};
OS   Maribacter aquivivus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=228958 {ECO:0000313|EMBL:SHJ78229.1, ECO:0000313|Proteomes:UP000184314};
RN   [1] {ECO:0000313|EMBL:SHJ78229.1, ECO:0000313|Proteomes:UP000184314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16478 {ECO:0000313|EMBL:SHJ78229.1,
RC   ECO:0000313|Proteomes:UP000184314};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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};
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DR   EMBL; FQZX01000001; SHJ78229.1; -; Genomic_DNA.
DR   RefSeq; WP_073242499.1; NZ_FQZX01000001.1.
DR   AlphaFoldDB; A0A1M6M444; -.
DR   STRING; 228958.SAMN04488007_1414; -.
DR   OrthoDB; 5522855at2; -.
DR   Proteomes; UP000184314; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00130; PAS; 5.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 5.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 8.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
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; 2.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08447; PAS_3; 6.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 8.
DR   SMART; SM00091; PAS; 7.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 8.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 5.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
FT   DOMAIN          211..263
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          338..390
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          543..589
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          592..644
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          846..898
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          973..1025
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1050..1260
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1260 AA;  144954 MW;  E6EA8BCE18590427 CRC64;
     MSTENTLLQT DKTSTTPSSI KNIGIFQFEV DSNKVTWNDV LREIHQVPKT FIPNADNIYG
     NCKEGIVKEN LIKAHTQALL KGVSFELEYE VITPKGSSRF LHVATHATTN DNKCTSLHGF
     ITDITHTKVK NIENHILKKQ LEYAEKLANS GSWKWDINLD TLTWSDNFYH ILKRHKEKPL
     SFETFLEYVH IEDKEEIAAK FDLALKTKHF PDSNYRIALK DGTIKNMKSI GEVITDAHGE
     VITIMGTCQD ITESKERDQQ LIQKKQQLEL TENSSEAGTW QLNTKTGAFK WSDNLYKITD
     FEYGEPISFE VLYARIHPKD KPHVDKALQS VKNTGIKKTF SHRLITRDKS IRTLEITADV
     VSNRINNDKV LIGTARDITD RIKIEHELIE KNQLLNFAEH LTTMGYWRYK PETDDVFWSD
     NLYQMFEQPK TDKLSFSTYF NKIHSDDKAF VKEKIDQSII DHKFYDFTHR IVLSDNTIRF
     IQILGKVTIN RNDGSQELLG TCLDVTDNES RELELSKKNQ QLNVAEKMAM IGYWQWNTTT
     NEVFWSDNLH AIYGHDKREP LTFETYINYI HKEDKKTVVA NLETAMKTGE FLESTYRIQL
     DDGSIKIIKS VGKITLNSKG EVLEMSGTCQ DITENKKKEL ELLEINRQLN LAEQMAMLGM
     WVWKPSKNIF KWSDSLYKIY GFELGSDVNI DKAISMIYTP DKEKVKEVIK NLLNGIEVPR
     STYRIIVNNN EIKTLEVRRE ISKDEHGNIE LLGTTQDITH IVETEQLLQE KNHLLSFTEE
     MASMGSWQWN PHTGISKWSD NLYKLYDLEL GVPIDMDLFL SRIHPEDSEK VVEHIEHIVA
     TQKSESLLSY RIVLNDDSIR SLELMAEVVK DSNGQMIELI GTAQDVTDRI KREQDLIEKN
     QLLTFAEQLS SIGYWKWDII QDVMEKSENL LKILDFEPGA KPDFKTYLKR VHPADREKVI
     DISQRIIETK KFDKFHHRIV KNDNSIKTIK LIGEVILDKE GNVIELIGSS QDITEQIEAH
     QKIMDTNRSL EKSTINLTSK NKQLAEFNHI TSHNLRSPVS NLNALLGLYK STENESKKIE
     IFEKFEIVID HLTETLNALI ETISIKNSAV EITQELCFEQ TLLKTKEILA AELIKSNANI
     RCDFSKAQNV RYNPIYLESI FLNLVSNSLK YRSEDRVPEI SITSNTVNGR ITLEFEDNGL
     GIDMKSNGHK LFGLNKVFHK HPDAKGIGLF LTKAQIVAMG GSISAKSKVD VGTTFFIILN
//
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