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Database: UniProt
Entry: I0K786_9BACT
LinkDB: I0K786_9BACT
Original site: I0K786_9BACT 
ID   I0K786_9BACT            Unreviewed;      1204 AA.
AC   I0K786;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=FAES_1980 {ECO:0000313|EMBL:CCG99989.1};
OS   Fibrella aestuarina BUZ 2.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Fibrella.
OX   NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCG99989.1, ECO:0000313|Proteomes:UP000011058};
RN   [1] {ECO:0000313|EMBL:CCG99989.1, 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};
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DR   EMBL; HE796683; CCG99989.1; -; Genomic_DNA.
DR   RefSeq; WP_015331088.1; NC_020054.1.
DR   AlphaFoldDB; I0K786; -.
DR   STRING; 1166018.FAES_1980; -.
DR   KEGG; fae:FAES_1980; -.
DR   PATRIC; fig|1166018.3.peg.3725; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG5278; Bacteria.
DR   HOGENOM; CLU_000445_127_1_10; -.
DR   OrthoDB; 9811889at2; -.
DR   Proteomes; UP000011058; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd19410; HK9-like_sensor; 1.
DR   CDD; cd00156; REC; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 3.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 3.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCG99989.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000011058};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          229..281
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          534..756
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          815..928
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          937..1053
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1083..1200
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          441..517
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         864
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         986
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1133
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1204 AA;  134072 MW;  B1EE8E6CC15C7BF6 CRC64;
     MPQLANSVIR QLQVVFSLST LLLLISLGAS FYSIRQLIDN SQLVNHTNQV LLESENIISY
     MKDAETGQRG YLVTLNRNFL QPYTGSYEKV QNSYEELRAL TRDNDVQQQA LTDIKALYDA
     KFAQMRRTIE LTERNPYFGR DTLNRNKEMM RGKQIMDDLR LKINRMKTEE QTLLKRRTEQ
     QQTYILFTPY LLVLTAIISI LITLFAYVRI KRDMDVRLAQ QLAAEAEYRR TNHRITVMEG
     ITRQIADGHY DVRSTDEQDD ELGRIAKALN GMAASLEQTF TDLKTKNWLQ QGVVRLGEAI
     RGEKGLDQLG ARLIDAIASY LKAPLGTLYL TDTDGTFKLA GSYAAQQPPA TVEAGVGLVG
     QAIATQKTTV VSGLPADYSP INSSLGSSAP STVVITPLVY DGTCVGAVEL GLLREPTEQE
     VHFLEQNSEM MAIGVNATLD FIRLQSLLEE TQTQAEELQM QHSEMENLNA ELEMQAQKLQ
     ASEEELRVQQ EELQQTNTEL EERGLLLEER NNDIQKKADE LELATRYKSE FLANMSHELR
     TPLNSILLLS RLLAENNEEN LTDDQIEYAK VIQGSGNGLL GLIDEILDLS KIEAGQMKLE
     FQDVAVADIT DELQALFGLL AKEKGLDFAI TVAPDVPSLI ETDRMRLGQI LKNLLSNALK
     FTSAGRIGLS ISRQAPDAGV LCFSVSDTGI GIPLEKQPLV FEAFQQADGS TKRKYGGTGL
     GLSISRELAK LLGGDLTLKS TVGEGSEFTL RLPLTDDVTV APPAPPVQPA FPAPATPPPP
     AVEAIPAPSD KRYISPTIPE AIPDDRATIA EGDKVILIIE DDTNFAKSLL DYARRKGYKG
     LVSVRGDEGL KLAAQYKPLG ILLDIQLPIM SGWEVMDALK ADPRTRPIPV HIMSSHKLKT
     ESRLKGAIDF VDKPMAFEQL QEVFKKIEYV LNRDPKKVLI IEDNPKHAKA LAYFLETFNI
     NSELKSNINE GVDALKRNEV DCVILDMGIP DHKAYETLEV AKKNPGLENL PIIIFTGKSL
     SMTEELKIKQ YADSIIVKTA HSYQRMLDEV SLFLHLVEEN KQASNNGPTK KLGALTQVLN
     GKTVLVADDD VRNIFSLSKA LEQYNMTVIP ALDGKEALQK LRENPGIGIV LLDMMMPQMD
     GYETARTIRE QYQWKNLPII AVTAKAMMGD REKCIEAGAS DYITKPVDID QLVSLLRVWL
     YDRS
//
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