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Database: UniProt
Entry: A0A0L0KNG4_9ACTN
LinkDB: A0A0L0KNG4_9ACTN
Original site: A0A0L0KNG4_9ACTN 
ID   A0A0L0KNG4_9ACTN        Unreviewed;      1270 AA.
AC   A0A0L0KNG4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Signal transduction histidine-protein kinase/phosphatase MprB {ECO:0000256|ARBA:ARBA00040454};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   AltName: Full=Mycobacterial persistence regulator B {ECO:0000256|ARBA:ARBA00041776};
GN   ORFNames=IQ63_03175 {ECO:0000313|EMBL:KND39398.1};
OS   Streptomyces acidiscabies.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=42234 {ECO:0000313|EMBL:KND39398.1, ECO:0000313|Proteomes:UP000037151};
RN   [1] {ECO:0000313|Proteomes:UP000037151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA   Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT   "Genome sequencing of plant-pathogenic Streptomyces species.";
RL   Submitted (JUL-2014) 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:KND39398.1}.
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DR   EMBL; JPPY01000023; KND39398.1; -; Genomic_DNA.
DR   RefSeq; WP_050369279.1; NZ_KQ257800.1.
DR   AlphaFoldDB; A0A0L0KNG4; -.
DR   PATRIC; fig|42234.21.peg.658; -.
DR   OrthoDB; 4652229at2; -.
DR   Proteomes; UP000037151; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR013587; Nitrate/nitrite_sensing.
DR   InterPro; IPR010910; Nitrate/nitrite_sensing_bac.
DR   PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR   PANTHER; PTHR44936:SF9; SENSOR PROTEIN RSTB; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08376; NIT; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50906; NIT; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037151};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        398..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          128..390
FT                   /note="NIT"
FT                   /evidence="ECO:0000259|PROSITE:PS50906"
FT   DOMAIN          421..491
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          608..714
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          808..1270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..68
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..869
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..899
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..954
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1033..1073
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1121..1141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1142..1163
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1214..1228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1251..1270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1270 AA;  132578 MW;  6DEE8BA4CFE79C00 CRC64;
     MQGRFKRDGS APAGPEPRGG TGAKTVSSSP QHAQNPGPAQ AGDGKSRPGA PTTPVTPTSI
     PPIPPAKPVK GDSGNRVALR NWRISTRLVA LLTLPVVAAT TLGALRINQS MEDIQQLDNM
     RLLTDMTKQA TELSIALQNE RDRSAGPLAH GGRADDATVK GLRTTTDRSL DAFVNASEEI
     DATSKNGNLQ GVRDNLVGLV GDLGNLAKLR STAYTAQGNA MQTVEGYHRL ITRLVDLSQD
     MAEATSNPEM IQRTRALAAF SSAKEYSSIQ RAVLTASLPA NNKVFGNLSD NDRNYGETAV
     EGEDSELAIF RSIYGDEGAE ELLKPIESGN ATIEEADQYA NRAYASDSGL ESQDKRSYQD
     WLDASGTKLQ QMRNIESQLL DDMEQKAREL RNETERDAII SGLLILMVLG VSLVGAFVVA
     RSMIRSLRRL QETATKVAQE RLPELVKQLS ESDPQDVDTS VESVGVHSRD EIGQVAAAFD
     DVHREAVRLA AEQALLRGNV NAMFTNLSRR SQGLIQRQLS LISELESREA DPDQLSSLFK
     LDHLATRMRR NGENLLVLAG EEPGRRWTRP VPLVDVLRAA ASEVEQYERI ELSSVPTTEV
     AGRVVNDLVH LLAELLENAT SFSSPQTKVK VTGHALPDGR VLIEIHDTGI GLSPEDLAAI
     NERLASPPTV DVSVSRRMGL FVVGRLSQRH GIRIQLRPSD SGGTTALVML PVDVAQGGKK
     PQPKPGQGGA QAGGPVAAQA AAGAAAARRQ GGPGQGAAGA FGGGPGGGKG AGFGPGPAGQ
     GSGAGAFGGG GAFGAGSGAG AGFGAGPGGG ALGGGPRTAL PGRDGAPARG QQQGGRPSAP
     APAGTGSFNG LQAAPPQGQP GQQQGQDMFG GGSRPPRGKD SRGGQDSRGG QDSRGGKGEQ
     GRGRQPQLPP RGGARAELPG GNSQPRTPSW GDENARPPAL DAPRGHDEPD VARTSQMPRI
     EGPGSTAEIP RVEGDFGRAN VNGAQHTGQF PALGAPAPQG NRRGAQDDFQ ATSQFPAIGG
     GQPGDAGGQF GRTEQEPVNN ANNMDNSGQF VRTDVFGTNP VPNTPQDTGQ FPARQQGYDA
     LPGRANANGY AAPQRPAVRP EPEALPPAGP GDGRTPLYDT LETNWFHQQG GQTQGVPQQP
     QAQAPAPAPT PAPAPPAPAA PQRPAAAPAA TASSSWRATP NDDLVRQAER VRQPASGGIT
     TSGLPRRVPR ANLVPGTAQQ QQHQAGPQVS RAPDDVRGRL TNLRRGIAQG RQAGSGQTDS
     FPSPTHQQER
//
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