ID A0A1I0F272_9BACT Unreviewed; 1407 AA.
AC A0A1I0F272;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04487998_2067 {ECO:0000313|EMBL:SET51309.1};
OS Hymenobacter actinosclerus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=82805 {ECO:0000313|EMBL:SET51309.1, ECO:0000313|Proteomes:UP000198697};
RN [1] {ECO:0000313|Proteomes:UP000198697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15310 {ECO:0000313|Proteomes:UP000198697};
RA Varghese N., Submissions S.;
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};
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; FOHS01000002; SET51309.1; -; Genomic_DNA.
DR STRING; 82805.SAMN04487998_2067; -.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000198697; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 4.
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; 5.
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; IPR013656; PAS_4.
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; 4.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; 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; PF08448; PAS_4; 2.
DR Pfam; PF13188; PAS_8; 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; 4.
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; 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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198697};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..65
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 166..237
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 294..364
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 661..713
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 714..785
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 785..839
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 857..1101
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1130..1248
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1310..1406
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1263..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1281
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1181
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1349
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1407 AA; 155614 MW; F40DFE63DBFCD36F CRC64;
MPSSPSNSAT PTSAALTPDL YRALFEQSAD GLLLYNAGGM LLDCNQRAVE YLGTTRARLL
GSGLMAFTAS AGPVPKGSPA TEAELRKALA AVAHSGEARS WRWLGPPAGG GAPLEAWVLV
SRLAGAAADG DSLLLLTLRD LQQHAPAAPF AAAVAETDAE PSESFSRGQL RDVLSRAGMC
YLLLDRQGVI QDVNTYFCEV TGHTTEALLG REYFGLFAPA DEQEPRRYAF QRALETQEVQ
DFFEHSLLTI YGRGRTFFWH SEFERDAAGA ITGVLFVGRD ITDKQVAVRA LTDNRNRLQD
FLDNAHDLIQ NLSIDNRFLF VNKAWKEKLG YDDDELPSLT LASVVHPYYK AKLLYQLRNL
YKGEKVNKLE TVFLTKSGKP VHLIGSISCS WQDSEPVSTR AILHDITDRI KAERLQKVYY
SIANLAISSK DLLSLYGAIH RELSKIIETN NFYIALCDEA RTQLQFAYFV DQNAPGEQAM
MTRPFSTGIS EYIIRTGRPL YLLREDLQKL VSGGMVTAYG LMPEVMLCSP LSIGERIIGV
IAVQDYQKAD AYAPSDIEIL HFISNQVALA IERKRNEVQI QKQNARLNAI FESGSHLMWS
LDTRARLASF NRNYAAYFLR RNGVYPALGM NMWQADVALM DPESREAFIS NYRRAFQGHP
QRFEVRLRDA KGQDSWREIY LNPIYLDDGS FEEISGIAHD ITDKKRSQLE LAAQEEKFRA
IFESFQDVYY RTDAQGLITL LSPSVYDMLG YQPEEVIGRF IGDFYTNPHE RDNLLQQVRE
LGEARNFEVA MRHKEGHAVS VLVNARRLLG DAENGQLNGT EGIGRDITGL KQMQDDLRLA
KEEAEQALEA KTLFLANMSH ELRTPMNGII GMIDLLHQTV ASEEQEEYVD TLRKSSDALL
AILNDILDLS KIQAGKLQLN DAGVDLHYTL EKIYSLFSNR ANQKRLKFTY HFTPTTPRFI
ITDETRLLQI LSNLTSNAIK FTSQGTVSII VSAVAAADVE DGAAADVVAD AAAGGAVEAG
KDDYLVRFAV QDSGIGISPD DEKLLFTNFT QLDTTPTKAF GGTGLGLAIS KQLADMLGGE
IGVYSNVGEG STFWFTIRCQ VALNEEEIVQ ERRLARERPQ EVVRFETNPR ILLVDDNPIN
QKVASRLLDK LGCTVTVAAD GFEAISRAIA PDTSYDLIFM DIQMPEMDGV TAMREIRRRL
GPSCPPVVAM TAYSMREDAK RFVEEGMDDY IAKPVKSQDL HAMLRRWSTP MARAVLSQVA
PAAPAASAPE TPAPAPETSP AAPPVEAVEA AAGIVVVDMA IVEQLRQLGG GEFAAQLYVD
FEQEAEQVLS EAAALVAAGQ YTAILPHLHQ LKGTGFTLGI MALAEGVKQL EQKLRDQDTA
STAVDFQLLL VLFAEFRAIY PALTQAP
//
