ID R7XSF7_9ACTN Unreviewed; 863 AA.
AC R7XSF7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=CF8_3916 {ECO:0000313|EMBL:EON22238.1};
OS Nocardioides sp. CF8.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=110319 {ECO:0000313|EMBL:EON22238.1, ECO:0000313|Proteomes:UP000015971};
RN [1] {ECO:0000313|EMBL:EON22238.1, ECO:0000313|Proteomes:UP000015971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF8 {ECO:0000313|EMBL:EON22238.1,
RC ECO:0000313|Proteomes:UP000015971};
RX PubMed=23833136;
RA Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT of Its Metabolic Capabilities.";
RL Genome Announc. 1:e00439-e00439(2013).
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EON22238.1}.
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DR EMBL; ASEP01000109; EON22238.1; -; Genomic_DNA.
DR RefSeq; WP_010834697.1; NZ_CM001852.1.
DR AlphaFoldDB; R7XSF7; -.
DR STRING; 110319.CF8_3916; -.
DR PATRIC; fig|110319.3.peg.485; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG2770; Bacteria.
DR HOGENOM; CLU_325116_0_0_11; -.
DR Proteomes; UP000015971; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR025291; DUF4153.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR Pfam; PF13687; DUF4153; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000015971};
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};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 554..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 597..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 641..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 672..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 713..732
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..112
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 120..329
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 328..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 90561 MW; A9570E5F572462E0 CRC64;
MKALLDAVTS IKVKLGALVA VSVVVVALLA TLGSSAGVPV WLTLPVAVLL TLGVTQLLAA
GMVAPLRSMT EVAQRMARGD YTGRVHTTST DEVGRLAAVF NQMAGDLALV EAERRDLIAT
VSHELRTPLA AMIAVLENLA DGVVPADAAH LDGALAQAER LRRLVADLLE LSRLEAGVTR
LQDTDVAVRP LVTDCLGEVS AAGRTGEFDV AVPEELVVRA DEARLRQLLV NVLDNAARHA
PNGSPVRIDA GRTPTGWWLT VADRGPGVDP SDRERVFQRF GTDPSGGGTG LGLAVARWVA
QLHGGTLRFT DPAPGRSGAL LRLELPDLSS PPEEATMTAP TTPPAPSVPP TYTPLPVEAP
TPPPGMDSFF GAFWPERPGL AGLRVVVASA LVGVLAGATM TFTAPGLSWV LVLLGAGTAA
YVTARHRRNA FTIGCTLLAS LLVLPLMLRD AEGIALLGVF AAAGVFLIGV TNARTPAGFL
LAGISWPLSS LRGLPWFGRA LRVVGTGGRT PAIVRTVVVS LLALGVFGAL FASADALFAT
WIDALVPTLS FNDLVTRVFV GCLVFAVTLA AAYLALNPSR VEPPRRVVEA LGNRFEWLVP
VLLVDAVFVL FLVAQATAVF GGHDYVERTT GLTYADYVHQ GFGQLTIATV LTLFVVWAAA
RKVRDAPTDR RWMRASLGLL CVLTLVVVGS ALHRMSLYQE AYGFTTLRLT VDVFEGWLGV
VVLLVMVVGG LGHGRWLPRI ALVTGAVAVL GLAAVNPDAW VAGRNLDRYE ATGQVDLVYL
QGLSADAAPV IAEGLPADVA ACVLRDLPGN QRSAENDDAL GWNLGRARAE DALAGLDLDA
TRPDAAGDPC GPIMDAYTAD PAG
//
