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Database: UniProt
Entry: A0A013VC59_9SPHN
LinkDB: A0A013VC59_9SPHN
Original site: A0A013VC59_9SPHN 
ID   A0A013VC59_9SPHN        Unreviewed;       342 AA.
AC   A0A013VC59;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=BF95_23620 {ECO:0000313|EMBL:EXS68934.1};
OS   Sphingobium sp. Ant17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1461752 {ECO:0000313|EMBL:EXS68934.1, ECO:0000313|Proteomes:UP000021537};
RN   [1] {ECO:0000313|EMBL:EXS68934.1, ECO:0000313|Proteomes:UP000021537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ant17 {ECO:0000313|EMBL:EXS68934.1,
RC   ECO:0000313|Proteomes:UP000021537};
RA   Adriaenssens E.M., Cowan D.A.;
RT   "Draft genome sequence of the aromatic hydrocarbon-degrading bacterium
RT   Sphingobium sp. strain Ant17 isolated from Antarctic soil.";
RL   Submitted (FEB-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=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:EXS68934.1}.
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DR   EMBL; JEMV01000052; EXS68934.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A013VC59; -.
DR   STRING; 1461752.BF95_23620; -.
DR   PATRIC; fig|1461752.3.peg.4135; -.
DR   Proteomes; UP000021537; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 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; 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   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        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          85..137
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          145..342
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   342 AA;  37321 MW;  0A1AA777A112D073 CRC64;
     MPEAGQVPLG LCFPDFSRTT ERAAGLVDAP RPDCWVVRFT DTTGERRALA LTFPRLAKPL
     RVIYNPLYLM VIIAASAGLA ILVARFVSKP LRRLERAAEA FSVSLDPEEI PERGPEEVRA
     ALSTFNLMQR RARAGFAERT QLLAAISHDL QTPMTRMRLR LELMEQGELR ARLLQDLQAM
     QTLVREGLDL ASSTEAREPW SLLDIDSLLA SMAEDAQELG APVRFMAGCG GTVRVKPNAL
     TRCIANLVDN AIKYGDSADI SCMRTGGRVL IHVRDRGPGI APDQLDQMFE PFTRGPSGQP
     GGRHGTGIGL TIARSLAMSF EASVRLRNAD DGGLIATIDM KG
//
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