ID V2JYN3_9BURK Unreviewed; 853 AA.
AC V2JYN3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Fragment;
GN ORFNames=B551_0211000 {ECO:0000313|EMBL:ESJ19228.1};
OS Cupriavidus sp. HPC(L).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESJ19228.1, ECO:0000313|Proteomes:UP000053474};
RN [1] {ECO:0000313|EMBL:ESJ19228.1, ECO:0000313|Proteomes:UP000053474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA Purohit H.J., Agarwal L.;
RT "Cupriavidus a Desert isolate.";
RL Submitted (AUG-2013) 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 -!- 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:ESJ19228.1}.
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DR EMBL; AMPR02000150; ESJ19228.1; -; Genomic_DNA.
DR AlphaFoldDB; V2JYN3; -.
DR Proteomes; UP000053474; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 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; 3.40.190.10; Periplasmic binding protein-like II; 3.
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; 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 PANTHER; PTHR43047:SF72; 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; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 1.
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; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000053474};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 383..603
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 633..754
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 781..853
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 119..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 684
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 820
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT NON_TER 853
FT /evidence="ECO:0000313|EMBL:ESJ19228.1"
SQ SEQUENCE 853 AA; 90155 MW; 40E7244154698F46 CRC64;
MSCGCLLWAA LVAAELGRTQ TPRDDTGAVR ERLAGTLTGA ERRWLAAHPV VRYSASPIGG
PMAFVGAGGH AAGIAVQALE QVGRITGLRF EPVWQQDPAA REAALRDGTV LLVPAVAADS
SAPPSVPQSA PPEAAAMRES GRRPHRLQPS LPYLITPWVI TTHATNVAIR DATALAGMRI
AVRRSNPGLT ARLAQVPNAT IIHTTSTSEA YRMVAHGQAD AAVDTLTCAH YMVRYAFAPR
LRVAAPLGPQ PAAIGFGVSP AAPQLRMILN KALAAIPPTH WDTLQAGWAS ASMPAAVPAP
VSARQRHRPW LLTGSLGTLL WMTAMGACAV ALHRHGRRIA RAATTLHRSL GGGRPAGRRA
TLPDVAASSG AWSGADRLGF LATICHEIRT PMHAVIGILD LLRHKAAIHG EARHYIDTAH
DCAKSLVALV GDLLDMARLE AGRMEIRPEP VQLDTLLQQW VHAFRPLASS RGLRIRLQLD
ALRARRHRAD PQRLRQVVGN LLSNAIKFGG HGDITVKLES AGEHVDRETV RIVVRDRGPG
IAAEQMPRLF EPFYRAAEAG GPGGTGLGLS ISRQLARQMG GELELISRPG HGTTALLTLT
LAAESCGGRA LHGHGRLTPC GQPAIAPLRK GYCALIVDDH PAGRMLLARQ LRHLGVEAVG
TGNAHEALVR FAAPDAAFDL VILDCNMPGM DGFTLARRLR AQERALARPR VPVFGYSADA
RPHNRQQALA AGMDDCLFKP IDLDTLDRAL QQWLADPPNG RRAAAAFTAT PLASASDAAS
DAASDAAIRA ALLAGNTADL AALRVAVARA DWQAAHAVAH RIKGAARLVS ADGVAQACEA
LEAACRDGDA AGV
//
