ID A0A0U2UGV1_9BACL Unreviewed; 483 AA.
AC A0A0U2UGV1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Signal transduction histidine kinase {ECO:0000313|EMBL:ALS22396.1};
GN ORFNames=IJ22_20220 {ECO:0000313|EMBL:ALS22396.1};
OS Paenibacillus naphthalenovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS22396.1, ECO:0000313|Proteomes:UP000061660};
RN [1] {ECO:0000313|Proteomes:UP000061660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660};
RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT "Complete genome sequences of two moderately thermophilic Paenibacillus
RT species.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALS22396.1, ECO:0000313|Proteomes:UP000061660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-Y {ECO:0000313|EMBL:ALS22396.1,
RC ECO:0000313|Proteomes:UP000061660};
RX PubMed=26868401;
RA Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL Genome Announc. 4:e01717-15(2016).
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; CP013652; ALS22396.1; -; Genomic_DNA.
DR RefSeq; WP_062408671.1; NZ_CP013652.1.
DR AlphaFoldDB; A0A0U2UGV1; -.
DR STRING; 162209.IJ22_20220; -.
DR KEGG; pnp:IJ22_20220; -.
DR PATRIC; fig|162209.4.peg.2140; -.
DR OrthoDB; 1948081at2; -.
DR Proteomes; UP000061660; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR037052; CheA-like_P2_sf.
DR InterPro; IPR035891; CheY-binding_CheA.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01627; Hpt; 1.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF55052; CheY-binding domain of CheA; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ALS22396.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000061660};
KW Transferase {ECO:0000313|EMBL:ALS22396.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 483 AA; 55979 MW; 9E45DC863D77486B CRC64;
MMDQLYVTYL EETEELLQKA EECLIRLETD YSSDDINALF RIFHSIKGSS QMIGHDDIGN
LTHKLEDMLD IVRKGRIDLD GQILQLCFSG LDHVKLMFES KKNQNDDGNN EVFTHAVEIL
EGKIVKILKA NSETENHRKA AFQGDSIVST LKGMERTGTN RYCICISFSD DIPMLSPILF
MIFNNIKDIG SLVYTNVSDE DIYEASANTQ IPSLVMIVES DWEEAELYTY FDVLYVEKVA
IADISEHQML KQATSLDQDS RRFFENFFLA FPKLYPVLFQ NRKDLSKAEY TELIHEPFQK
ILEKVDKIPV SAVEKKLKQE IETFYDLCLH ATSGKSALQV ETIELLCQKY LELFEMAYAD
VKGKFFYKIF KVKGSHFIDH LKGFIERMNK SCTRKLLLDL SRLEMIHEHE LKSLIELKRR
LHDMGIVMSV VIDSRLRKRL INIFDSIQTI EHFALFDTEV DAALGDHISV LVNEKRCMED
FMK
//
