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Database: UniProt
Entry: A0A0T6UL59_9PSED
LinkDB: A0A0T6UL59_9PSED
Original site: A0A0T6UL59_9PSED 
ID   A0A0T6UL59_9PSED        Unreviewed;      1151 AA.
AC   A0A0T6UL59;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AO726_17055 {ECO:0000313|EMBL:KRW58548.1};
OS   Pseudomonas sp. TTU2014-080ASC.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1729724 {ECO:0000313|EMBL:KRW58548.1, ECO:0000313|Proteomes:UP000051864};
RN   [1] {ECO:0000313|EMBL:KRW58548.1, ECO:0000313|Proteomes:UP000051864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTU2014-080ASC {ECO:0000313|EMBL:KRW58548.1,
RC   ECO:0000313|Proteomes:UP000051864};
RA   Webb H.E., Bugarel M., Den Bakker H.C., Nightingale K., Granier S.A.,
RA   Loneragan G.H.;
RT   "Carbapenem-non-susceptible Bacteria Recovered from the Faeces of Dairy
RT   Cattle.";
RL   Submitted (SEP-2015) 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}.
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:KRW58548.1}.
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DR   EMBL; LKKK01000013; KRW58548.1; -; Genomic_DNA.
DR   RefSeq; WP_058069331.1; NZ_LKKK01000013.1.
DR   AlphaFoldDB; A0A0T6UL59; -.
DR   STRING; 1729724.AO726_17055; -.
DR   OrthoDB; 9797243at2; -.
DR   Proteomes; UP000051864; 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   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00088; HPT; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd13705; PBP2_BvgS_D1; 1.
DR   CDD; cd13707; PBP2_BvgS_D2; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 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; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; 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   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF5; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00497; SBP_bac_3; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00073; HPT; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00062; PBPb; 2.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 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; 1.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051864};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          513..585
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          587..639
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          657..882
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          905..1024
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1053..1148
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         954
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1092
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1151 AA;  127281 MW;  12F2C6F67DA6B399 CRC64;
     MGVSRPDHRP FDITTSDKQY EGVSADYVDL LRQTLDIPFD ITIFEDRKQA RQALINGTVD
     LLASSNNFDI QDVSLTLTQH YAPDQIALYV RLNEKRTFPE YFNGVKIAIP DDYLTPATIR
     EFFPHALIET YNSRHEALAA LAFGKADLYL GDSYSANLII NEQYFNYITI ERLLHTHPSG
     TSFAIRKDND TLLEIINTAI QAISPHDSRE ILRRWGGGTG SSITQPLELS ASEQNWLRRH
     PEIAVAIGLD QAPIAFIDQD DNFGGVMSDL LKIVTLRTGL KFNVRTYGKG LDLINALNNN
     QADLAALSPS ITREATLRFS LPFAVMPFGL VVNQDNNEVS DLPSLAGQRV AIPNGHILLE
     YLKDLHGIQV IRSNNFVEAL DLASSGKADV AIAPLMIARY YLLHTKDLNL KISGIIGPDK
     AKFSFATSRA NTELESILNK VLRELPPDEL NVINTRWRAN SAMRESRLVD YQSMILKIAA
     LVCILIAAAF IWNLKLRRQV QQRRAAEHAL GDQLRFMRTL IDGTPLPIYV RDRDGKLLTC
     NQSYTSSLGL CDDDVTGKTA IEEGAVLPEE ARRFHADYLL AIQTGEPLVK DRTLHVDEQT
     FHIYHWIQPY RNRRGEVQGV ICGWLDISER HQLVSDLQAA KQQADDASRA KTTFLATMSH
     EIRTPMSAVI GMLELALKKR ATEGFFDTSA IEVAYSSAKG LLELIGDILD IVRIESGRLN
     LAPRRTNLRE LAKSVIRVFD GLARQKGLTL TLDFDFGPGA KTDVLVDPVR IKQILSNLIS
     NAIKFTDIGQ VQLNIKGTPL PDERIRLNVR VADTGLGISA QDQAQLFKPF SQATQTTTGA
     RGGTGLGLSI CRSLCEMMGG SLNLSSELGV GTVVTFDLTL SCLPEAKATS SADTERLSSD
     SHSLNVLVVD DHPANLMLLA QQLEFLGHVV TKASNGSEAL EHWHKQTFDL IITDCNMPIM
     SGYELAEAVR LDESMRGINP CSIFGYTANA QPEEQERCLR AGMNKCLFKP ISLEELSECT
     GSIAPTPQET TSDGADDMDT FNIAATYQLT RGDKTLAAQL LNELVRSNRS DLDELQTMAG
     KFDLTGVASL AHRVRGAARI VQAKHLIEAC MELEAAAKSH DTTPEHLAEA VQSLKMTIEN
     LERAILATQH D
//
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