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
//