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Database: UniProt
Entry: A0A2R4CD21_9BURK
LinkDB: A0A2R4CD21_9BURK
Original site: A0A2R4CD21_9BURK 
ID   A0A2R4CD21_9BURK        Unreviewed;      1160 AA.
AC   A0A2R4CD21;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C9I28_19050 {ECO:0000313|EMBL:AVR97506.1};
OS   Pseudoduganella armeniaca.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Pseudoduganella.
OX   NCBI_TaxID=2072590 {ECO:0000313|EMBL:AVR97506.1, ECO:0000313|Proteomes:UP000240505};
RN   [1] {ECO:0000313|EMBL:AVR97506.1, ECO:0000313|Proteomes:UP000240505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZMN-3 {ECO:0000313|EMBL:AVR97506.1,
RC   ECO:0000313|Proteomes:UP000240505};
RA   Huang H., Ren M.;
RT   "Massilia armeniaca sp. nov., isolated from desert soil.";
RL   Submitted (MAR-2018) 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}.
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DR   EMBL; CP028324; AVR97506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R4CD21; -.
DR   KEGG; masz:C9I28_19050; -.
DR   OrthoDB; 5290456at2; -.
DR   Proteomes; UP000240505; Chromosome.
DR   GO; GO:0016020; C:membrane; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.60.40.2380; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF07696; 7TMR-DISMED2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000240505};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..1160
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015347249"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        352..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          427..648
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          666..788
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          817..933
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          978..1079
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         720
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         866
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1017
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1160 AA;  123324 MW;  313689A92BBB4A9C CRC64;
     MTRAAAHRPL APFVTVLCAL CCWLGGLLLA QAAVAAPTPL VVDPNVGAID AWPALTVLDD
     PRGELTPAQA LAAADRFEPP RTANATLGVE PHLVWLRIPI VVPPGGDTHR VLAIDYALLN
     RVDVYLATGS AIVAHPPAGN MLPAGQRGLS GRVPAVSLHL TPGASHTILV RAQTSAPILL
     PIQLYTPEGF HAAALDEHML QGLMLGLGLC LLLYSLAQWA NLREPLFGKY ALLVGGITLY
     SADFFGIGAQ YLWPGNAWMT QHAGGLLSLA ASCGAYLFVQ QALARPGMDR VYSRLMRIGA
     ALCVLTAIGF AFDLVDVETL VLFISTLGIM PMLLGLPKAF ARARRGDTVG SYFLVGWSIS
     FVSSVILTLV FKGLLGANFW TMHALQFGST IDMLLFMRIL GLRTKAMQNA MLRAEEATRM
     KSDFLANMSH EIRTPMNAII GMSRLALMAD PNPKQRNYLD KILGAGEHLL GIINDILDFS
     KIEAGKLVLE AVPFDLNELF DHLSNLTAIK TDARRVELVF RIGRGIPGRL VGDPLRLGQV
     LINLTNNAVK FTEEGEIVVA VSVVQRAPGT IVLRFSVTDT GIGMNEEQLA RLFQSFSQAD
     TSITRKYGGT GLGLSISQQL VELMGGRIKV ASTPGTGSQF SFSVPLGVAD PGQQPVTPSA
     PLHNARVMVV DDSTTAREAL VEMLGSLGVH ATGIESGEAA LAELAAAMLA GNPYQVVLMD
     YMMPGWDGVE TIRRIRSDRR FAAPPAILMI SAATRDAVLQ QEGLVPMNGF LHKPVGPALL
     YHTLLQVLRP ELAEPGEVGR AQAPSARLDL SRLDGARILL VEDNANNREV ALDFLAAARM
     QVDVAVHGAD AVRMVAEGDY DLVLMDIQMH VMDGLTATRE IRATIGAREL PIVAMTAHAM
     AGDRERSLAA GMNDHITKPI DPDQLFRTLL KWIPPGRLAG RSLAALPAAD LPDAGATAAL
     PVIGGVDWAR AGTGGDQWQA RLFKRIRSFR GEYGGAAAQV REALAAGTPA ALQALAHNLK
     ASAAYIGAWR VAGLADQLEQ ELRGPARNER ALALAGELAD ALEPLLAGLA GLAQVEPPAP
     AAPARADAGD LIRLLAGYLR SDDARAEDAV QALQALLADS PHGGLLATVA RAIDDIEYDA
     ALAPLAALAQ ALDVNMEENA
//
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