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Database: UniProt
Entry: A0A1I5YIN9_9BACT
LinkDB: A0A1I5YIN9_9BACT
Original site: A0A1I5YIN9_9BACT 
ID   A0A1I5YIN9_9BACT        Unreviewed;      1128 AA.
AC   A0A1I5YIN9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04515674_11918 {ECO:0000313|EMBL:SFQ44069.1};
OS   Pseudarcicella hirudinis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Pseudarcicella.
OX   NCBI_TaxID=1079859 {ECO:0000313|EMBL:SFQ44069.1, ECO:0000313|Proteomes:UP000199306};
RN   [1] {ECO:0000313|EMBL:SFQ44069.1, ECO:0000313|Proteomes:UP000199306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E92,LMG 26720,CCM 7988 {ECO:0000313|Proteomes:UP000199306};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOXH01000019; SFQ44069.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5YIN9; -.
DR   STRING; 1079859.SAMN04515674_11918; -.
DR   OrthoDB; 9811889at2; -.
DR   Proteomes; UP000199306; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00088; HPT; 1.
DR   CDD; cd00130; PAS; 2.
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; -; 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; 3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; 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; 2.
DR   PANTHER; PTHR45339:SF4; HISTIDINE KINASE CONTAINING CHEY-HOMOLOGOUS RECEIVER DOMAIN AND PAS DOMAIN-RELATED; 1.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
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; SSF55781; GAF domain-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); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199306};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          42..109
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          113..164
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          165..235
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          532..584
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          602..823
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          850..969
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1028..1128
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   COILED          1097..1124
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         902
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1067
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1128 AA;  128707 MW;  0A8F0CFC62063F0A CRC64;
     MRWSHKSKEQ LITEIRHLKK ELAVLENNDK ANFFTPKAGF DIAKTVESLN LVGLILEADG
     NIVFCNTFTE KALGWTAEEL VGQNFFDVLV PPSQREQRLD AFKTAMENGG IFGTKERTLL
     AKNGQTRYIE LNSTIFNSAG EDQYLTIIGE DVTERRKVSE ALTRSNSQLQ DLVNNTSDLV
     QIISISGRFL YVNKSWQESM GYQSDELTSL KLKDVLHPDF AEDTLHKLER VKNGEKIPDF
     ETVFRRKDGR RLYLSGSVNC RFEKDVPTAF RCIFHNSTAK VRAERATKLY SSIAQTTINS
     TNLDNLYENI HKELGEVIDV KNFFIAQYDP AKSFLYFPYY IDEYFDSRVH FTKRKLGNGL
     TEYAIMANQP LILQDVDIQR LAEEKKIYLY GVVPKVMLCV PLRIGDRVTG IIGVKSYERT
     NKYERKDLEL LDFISRQVAL AIERKQAEEA LARETARLNA IFEGSSHLMW SVNRKMLLTS
     FNQEYSNLLA SQINVRPQLT LSTESMGFRM LSAPDRRILE EKYKQAFKGF QQHFELQLET
     ALGDEKWVEI YLNPILLNND VIEEVSGIGR DITDLKKYQQ DIVKAKDEAE RSLKVKERFL
     ANMSHEIRTP MNGVIGMIDL LNDTPLDIEQ KDYVQTIKKS SETLLHILND ILDLAKIEAG
     KMVLHEAPLV FRDLFDRLLA LFSQIAANKR NKIVCEFGEN LPEFVIADET RLLQILSNLT
     SNALKFTENG VVRIKINLLE KRGKFNRLKV EVLDSGIGIT RENLAILFNA FQQVDNSTTK
     TFGGTGLGLA ISKELCRLMK GEIGVESELG EGSNFWFTVE LKQTDISPSM MIRNNDEFHI
     VDHFKNYQPH LLLVDDNATN RKVASQILIK AGCKVITADS GMKAIELVKS SVNERFDLIL
     MDIQMPEMDG IETTKRLREM EGAGLPPVVA MTAYAMKEDR DRFLSNGMND YISKPIRAEN
     LVRKVKEWVD KKLSVKTVTS VSDQEKPKSE ENLVAEAGSP ELFEEILKKL PVLDNEILKQ
     LADSVGGEMD FVVSILEGFE EEALEQIRNA KTGFLENDCR AVQSELHTLK GNSGTLGVMR
     LHEITRHIEV KAKVCDFRDF EEEIRILESE FEAFQEVYRE LAQKVSEK
//
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