ID A0A0V8TAH1_9CELL Unreviewed; 362 AA.
AC A0A0V8TAH1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-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=ATM99_06975 {ECO:0000313|EMBL:KSW29652.1};
OS Cellulomonas sp. B6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW29652.1, ECO:0000313|Proteomes:UP000054319};
RN [1] {ECO:0000313|EMBL:KSW29652.1, ECO:0000313|Proteomes:UP000054319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:KSW29652.1,
RC ECO:0000313|Proteomes:UP000054319};
RA Piccinni F.E., Campos E.;
RT "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas strain
RT Isolated from Decaying Forest Soil.";
RL Submitted (NOV-2015) 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=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:KSW29652.1}.
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DR EMBL; LNTD01000051; KSW29652.1; -; Genomic_DNA.
DR RefSeq; WP_062101580.1; NZ_LNTD01000051.1.
DR AlphaFoldDB; A0A0V8TAH1; -.
DR STRING; 1295626.ATM99_06975; -.
DR OrthoDB; 9757990at2; -.
DR Proteomes; UP000054319; Unassembled WGS sequence.
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; 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; 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, ECO:0000313|EMBL:KSW29652.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054319};
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 36..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..133
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 141..358
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 362 AA; 38889 MW; 467E966F4FBD2556 CRC64;
MTSPPSPPAR HARGDDRWHL PDVRPLDPLR SIKIKLGVLV ASTVTLAAFV IWVGYGRALG
PSRTLPLAIV LSLIVTQLLA RGMTSPLREM TMAARAMAGG DYSRRVRSTS RDEVGQLAEA
FNTMADDLQN LDTFRRELVA NVSHELRTPV TALQAQLENM VDGVSEPDPA TLATALAQTE
RLSRLVSSLL DLSRVEAGAM ELRTQDVPLA RLLGEATDEA SLVGAAKRLR FGVDVEPPDL
TVPADPERLH QVVANLLQNA ARHSPEDDEV TVVARRVGED VQIDVVDHGP GIAREQRAHV
FERFVRGNTP ALTGQGSTGG TGLGLAIVRW AVELHGGTVE VADSPSGCTM RVRLPAAPAT
RP
//
