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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//