ID I0KF55_9BACT Unreviewed; 1127 AA.
AC I0KF55;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=FAES_4759 {ECO:0000313|EMBL:CCH02758.1};
OS Fibrella aestuarina BUZ 2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCH02758.1, ECO:0000313|Proteomes:UP000011058};
RN [1] {ECO:0000313|EMBL:CCH02758.1, ECO:0000313|Proteomes:UP000011058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX PubMed=22689241; DOI=10.1128/JB.00550-12;
RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT Bacterium.";
RL J. Bacteriol. 194:3555-3555(2012).
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HE796683; CCH02758.1; -; Genomic_DNA.
DR RefSeq; WP_015333857.1; NC_020054.1.
DR AlphaFoldDB; I0KF55; -.
DR STRING; 1166018.FAES_4759; -.
DR KEGG; fae:FAES_4759; -.
DR PATRIC; fig|1166018.3.peg.1728; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_000445_114_15_10; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000011058; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
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; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13188; PAS_8; 1.
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; 3.
DR SMART; SM00091; PAS; 4.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CCH02758.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000011058};
KW Transferase {ECO:0000313|EMBL:CCH02758.1}.
FT DOMAIN 243..296
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 321..371
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 368..414
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 442..494
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 571..624
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 642..864
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 887..1002
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1032..1126
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 29..81
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 936
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1071
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1127 AA; 126857 MW; 30B1C12B5AFAEABA CRC64;
MSYHKLLQKQ IARYLPDDLQ AEPAMARLLE VVSESYRALE RDRELAERAF TISEDEYVQL
NNRLQHELDV KKLSVEKLTE AVSTISGADI QYDADDLLGI ARLLNQQVSK RKNAEEVFTS
LIANMRSGVV LEDEQQQVVF INQVFCDLFG IDTPPQQLSG THGQVLTDRI NQQAKAPHVV
SRDMANTLAN RWLVQGYMLE LATGKTYQRD YIPIYIDDAY KGHLWSYTDI TERKANQDAL
VQSELKNRLI MNAALDAIVT IDTEGLITFW NPQAEKIFGW AAADVIGRKI AEVIIPPTHR
AAHEAGMANY RTTGIGDVLG KQMELPAINR AGDLFPIELY IIPVNQGDDT FFCSFIRDIS
ARKKAETELE RLSLVASANK NGVVLVGRDG RIFWSNEGFC RLTAYDNDEI IGRTPMELCR
GPFSDREALK TMVNSFEKGI PFDIEGIHYR KDGSWFWGRT EGQPVADEAG TVTHYFSIIE
DISAEKVAQR KLKEYEERLR MALTNVGDNY WEHDFRTGRT YFSNPSNNLL GYQLDKHIDV
AGLWWSRVHP DDRRLLEEND RQYKLGLISH HHNEYRIIHR DESVHWVLDR GVVTEKDGDN
KPLKIIGTHI DITRQKELEL ELTKAKDAAE ELARVKELFL ANMSHEIRTP MNAIMGMANR
LSKTSLHPDQ QYYLSIIQSA TDNLLIIIND ILDLSKIEAG KLTLEKIGFE PKQVIDRAMQ
VMVHKAEEKG LLFTNAFFDP RIAPVLLGDP YRLNQILLNL LSNAIKFTQK GHVNVSCHLL
KGSRNQQLIE LTVSDSGIGM DEAFTKRIFQ TFRQEDESVT RRFGGTGLGL SISHNLVELM
GGTMQVKSKK GVGTSVSFQV PFPKGDPDKL PVKEAEVTDT DRLLGKRILV ADDNEMNRLV
ASTMLSSYGA IIEEAQNGVD ALDKLKQQAF DLVLMDIQMP VMDGVEATRI IRADISAQLP
VIALTAFAVK GDSAKFIGAG LSDYLAKPFS EEQLLAIVVR WLEKAEAALL PAAAPEPPLY
DLSTVMNLAK GNQAFVDRMV DLFMRYGPES VQEIRAAYAA GQFEQVRKVA HRVKPSIDNM
GISSLTADIR AIEANAETWQ TSPELETLID KLDRVMNVVV EQLKARA
//
