ID A0A1C0ZYT1_9BACL Unreviewed; 1266 AA.
AC A0A1C0ZYT1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A8709_03285 {ECO:0000313|EMBL:OCT13293.1};
OS Paenibacillus pectinilyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=512399 {ECO:0000313|EMBL:OCT13293.1, ECO:0000313|Proteomes:UP000093309};
RN [1] {ECO:0000313|Proteomes:UP000093309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC13222 {ECO:0000313|Proteomes:UP000093309};
RA Zhang J., Zhang X.;
RT "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL Submitted (MAY-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCT13293.1}.
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DR EMBL; LYPC01000023; OCT13293.1; -; Genomic_DNA.
DR RefSeq; WP_065854108.1; NZ_LYPC01000023.1.
DR AlphaFoldDB; A0A1C0ZYT1; -.
DR STRING; 512399.A8709_03285; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000093309; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; cd00130; PAS; 2.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.340.10; -; 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; IPR033479; dCache_1.
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; 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; 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; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF158472; HAMP 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); 2.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
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, 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:UP000093309};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 275..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 300..353
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 440..492
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 489..527
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 631..852
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 867..984
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1022..1139
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1162..1260
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 916
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1072
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1201
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1266 AA; 141827 MW; B53318C7EA85A31A CRC64;
MSSSLRFKLV AWLVLLTSIS LAVVGITNYT LSRNKLLHQI NEQSITSVSN SAQNLYDFLS
IRLAEVELIS RVSIMKKGTQ AERLSFLTQE LKTDEKRYYA MAISDLSGTL EFTSGITISM
TGERRFEQAL QGNTFISDPH MSKMKGVYVI SITAPIFDDE HKVVSIIDVS LRADPTFQEH
LLPPLDNGEL LLVNQNGLTL YDSEASSILN TNIFTDYPKL NPEFQKGLLK GKGYIDESIL
SGQKTRWFYS RVPHLDWYLA YSMPITTIEA PTSPLLWSTI GLIVMTALII FILIYIVTNH
LIIKRIKQIL QVTEAVAAGD FHTKPIVFTS KDELGALALS VNGMMENLRE LFEPFEAFIH
HNQYAMIVMD PNYLINHLNG RAVELLGYSL SEVHKSASPL IWLDQQQVTE RAAQYSIELG
EIIPADCTAL VIRSLRHLKE DSEWTWYHKD GARIYVQASV SCITHPNGEL KGYVLIARDI
SDIKKSNEMK ERLLTIVESA RDMILTFDQE GYIFYINQAG IRTIGLEHTP VGRTHFSEYV
EILNTIDLNE GLLAAIQLGF WEFEAEVLTK NQQRLTVSLI IVPHYPIDNG ELYFSAITRD
ISDQVRAKEE LILAKQEADE ANLAKGVFLA RMSHEIRTPL NGIVGLSHLL EKTAMTDLQK
DYIRKISRSS RSLSHIINDI LDFSKLEVDK LVIEHHPFQL DETIDRVCET LSVQLGHKPV
DFICDIPNHV PTSLIGDSLR LYQVLLNLAS NAIKFTEFGT VTLRVQIDQQ NEQEVSLLFR
ISDTGIGMDE QQLAILFQPF VQGDDVTSRK YGGTGLGLVI SKNIIENMGG AISVTSTQDA
GSEFVVALTF ALNLPMSSKV LTPLPVTVLV VEDHPELNPV LVHSLQSICT DVAGVLSWKE
AFQVIEHVPL DMILLDMEAD DMYGEDVWLN MLAACKRHGI RTIVYTSLSG RDALEQLPIT
AAPDAILVKP ISRSLLYRTI DSLTSEQEEM SRNLSLHEHV NQNLDKPAHS LTFSALADTP
LHILLVEDND INQTVARSLL ESMMNCRIQV AGNGFDALHD LENDTYDLIL MDIHLPGLDG
IETTKRIRLE PKWAHIPIIA ITADSTLDNR LACMAAGMSE MISKPIIPER LQSVIEAVLQ
QHAAIRSDDL DIAQALQRIG GRTDIFREML RRFQEQSIPL MEQLILAIGT GDHEEALRLL
HGLRGSSSNL SANRVFAAAT ALEEHLKENG FTPSVNDTGP SLLDHLQKVE DELRNVFLAI
QKLLLD
//
