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Database: UniProt
Entry: A0A243SCB9_9FLAO
LinkDB: A0A243SCB9_9FLAO
Original site: A0A243SCB9_9FLAO 
ID   A0A243SCB9_9FLAO        Unreviewed;      1064 AA.
AC   A0A243SCB9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=FPG59_14795 {ECO:0000313|EMBL:OUD31769.1};
OS   Flavobacterium sp. FPG59.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1929267 {ECO:0000313|EMBL:OUD31769.1, ECO:0000313|Proteomes:UP000195161};
RN   [1] {ECO:0000313|EMBL:OUD31769.1, ECO:0000313|Proteomes:UP000195161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FPG59 {ECO:0000313|EMBL:OUD31769.1};
RA   Wu A., Liu R., Kropinski A.M., Macinnes J.I.;
RT   "The genome of Flavobacter psychrophilum strain FPG59.";
RL   Submitted (DEC-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:OUD31769.1}.
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DR   EMBL; MTCA01000270; OUD31769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A243SCB9; -.
DR   OrthoDB; 9766459at2; -.
DR   Proteomes; UP000195161; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 5.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-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; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000195161}.
FT   DOMAIN          558..628
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          631..683
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          701..922
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          945..1060
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         994
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1064 AA;  120572 MW;  5BCD93D7A98B770E CRC64;
     MDAKDYIRIF EQSPALMLVI DTSFIIIAAS DDFIRKTKTT RECITGQNIF YVFPSNPDNT
     NRNEESTIRA SFNRVIKNKT ADTLPVIRYD IPKPASEGGG FKTKYWKVVN SPILDHNNNV
     QYIIQRSDDV TENETLVAQL DAEQKAIKQL EESEKRYYMM LLKSPFGFAI LKGKNMVITL
     ANDSVKEMWG KGNDLEGKTL LEVLPEIKDS EFPDLLDKVY TSGTPFCGDE VLCPVFRNGK
     LEDVYFNFVY QPYLEADETI SGITIIAYEV TAAVIVKNAL AALHNADLKA LKKIEEISNR
     YYMMLMDSPF AFCVMKGKDM LVTLANDLMK DFWGKGKDVE DKTLLEILPE IKDQPFPEMI
     DKVYTTGIPF YANEILGKVT YNGKLKHKYF NVVFQPYYDA DNSISGVTQI AYEVTEMVMA
     RKKIEESDKR YNMMLMNSPF TFAVLKGKDL IIELANDQIK EVWGRGNDIE GKSLLEIMPE
     LKNTTFLDML DEVRATGIPF HGIEVQSPKN MHGTIKEEYF FNFVFQPYLE ADQTISGITI
     IGNEVTEQVI AKRGIIENEK KLRQILDSMP QKITNADTEG NVIYFNKKWL DDTGLEFEKL
     KGWGWEKVIH PDDVEMTKTN WSNSFKTGEI FDMECRILHK DGAYKWHLSR ALPIKDEHGK
     IKMWVGTNTD IHEQKDAKYK AETAQIAAED AMQAKQQFLS NMSHEIRTPM NAIIGFTNVL
     LKSKLDQSQK DYLTAIKDSG DALLVLINDI LDLAKVDAGK MTFEQTPFNL ADSLSSMLQL
     FDMKIKEKNL ELITQFDIAI PEIIMGDSIR LRQIILNLIS NAVKFTNAGK ITICVSLLKQ
     DAEEITIDFT ITDTGIGIHK TKLEHIFEDF GQATYENSRL YGGTGLGLTI VKKLIEQQGG
     TIHVQSELGK GSAFSFLLNF AKTNQKIEQQ TEPVSNIQAE VKKINILVAE DMPLNQLLIK
     IILADFGFDV DIAANGKIAI EKLKQNKYDL VLMDLQMPEM NGFDATAYVR NIMKSDIPII
     ALTADVTSVD LEKAQAMGMN DYVSKPVDEQ LLYSKIIKAL QKTD
//
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