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Entry: A0A2Z6EUQ3_9BURK
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ID   A0A2Z6EUQ3_9BURK        Unreviewed;       847 AA.
AC   A0A2Z6EUQ3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=GCM10007934_16720 {ECO:0000313|EMBL:GLR01860.1}, MCB1EB_1032
GN   {ECO:0000313|EMBL:BBE09193.1};
OS   Mycoavidus cysteinexigens.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Mycoavidus.
OX   NCBI_TaxID=1553431 {ECO:0000313|EMBL:BBE09193.1, ECO:0000313|Proteomes:UP000282597};
RN   [1] {ECO:0000313|EMBL:BBE09193.1, ECO:0000313|Proteomes:UP000282597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1-EB {ECO:0000313|EMBL:BBE09193.1,
RC   ECO:0000313|Proteomes:UP000282597};
RX   PubMed=29540638; DOI=10.1264/jsme2.ME17138;
RA   Sharmin D., Guo Y., Nishizawa T., Ohshima S., Sato Y., Takashima Y.,
RA   Narisawa K., Ohta H.;
RT   "Comparative Genomic Insights into Endofungal Lifestyles of Two Bacterial
RT   Endosymbionts, Mycoavidus cysteinexigens and Burkholderia rhizoxinica.";
RL   Microbes Environ. 33:66-76(2018).
RN   [2] {ECO:0000313|EMBL:GLR01860.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 110909 {ECO:0000313|EMBL:GLR01860.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [3] {ECO:0000313|EMBL:GLR01860.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 110909 {ECO:0000313|EMBL:GLR01860.1};
RA   Sun Q., Mori K.;
RT   "Draft genome sequence of Mycoavidus cysteinexigens strain NBRC 110909.";
RL   Submitted (JAN-2023) 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};
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DR   EMBL; AP018150; BBE09193.1; -; Genomic_DNA.
DR   EMBL; BSOD01000035; GLR01860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z6EUQ3; -.
DR   KEGG; mcys:MCB1EB_1032; -.
DR   Proteomes; UP000282597; Chromosome.
DR   Proteomes; UP001156688; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00088; HPT; 1.
DR   CDD; cd01007; PBP2_BvgS_HisK_like; 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; 2.
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; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE 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   Kinase {ECO:0000313|EMBL:BBE09193.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000282597};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000313|EMBL:BBE09193.1}.
FT   DOMAIN          333..553
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          598..719
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          754..847
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         647
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         793
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   847 AA;  93466 MW;  396741921CCC70DB CRC64;
     MSIYLDRKLC YSLWLAVTLI ISTHVYSAEK KICFSAEERV WLEQRPVVRI AVAPDWGPIE
     FIEHGQHQGL TAGYLQAITQ ISGLQFQLVP TRSLQASLKK LRAGQVDLLP VAYGFPEVDE
     ALGYVRCTRP YFSGSSVVIT KGETPVTGDL RQLAGHVVAI SNSAFYAYWL RQYHPDIKVL
     QVTSPEAALS AVAKNKAYAA LGFGMNFHHL MKTKYRGILF YSSKVPNLPI IGRMGVRGDL
     VLLRDILDKS LAMLSAAQKD EIEQRWIYLS PQPAKTQPAP QIVASQTSFY SIYNEALVLA
     VSSIIFICLV FHLWQTHKKA SETVKEKSML LAIFSHELRT PISAIISAVE MLKRFSGDAR
     RQSRLIAVTE STAQSLLLLL NDTLNNAGDL SFKKTPVQPA ELAKEVVDVV AAPAANKHLP
     IFIQISENLP ERICLDVLRF KQICVNLLAN AVKFTDTGSV TLKLAIDKSD FVENTAELIL
     SVCDTGIGIC PQQQTRLFRP FSQANHSIAR RYGGSGLGLA ISNKLAKRMG GYIMINSVPN
     QGTTASVRVP IQVLKWHSEA GASQDERPCV PTQTQQNAKQ PPLLSVTQPA AAPRAVPKVL
     LIEDHIAIQS VVLEQITLLG YHAVLATHGA QGLKIWQEQE FPIVLVDCSL PDMDGYTVAR
     EIRSIERERG PLYPYTALFA LSAATDDAHQ MQCLTSGMDG VLSKPLESEV LQRILAVWAP
     LPTLENNFES LAHQSAAFSE ANGLEGVKET TRTPSEDPHH LITRFQQTTV QDIHQLNAAL
     NQCDMEGVAR YAHRIKGSAL MFKFSSIADT ADQLETSARS RSTDRARLDK ALQALREACN
     GQLYPLT
//
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