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Database: UniProt
Entry: A0A261SNI3_9BORD
LinkDB: A0A261SNI3_9BORD
Original site: A0A261SNI3_9BORD 
ID   A0A261SNI3_9BORD        Unreviewed;       508 AA.
AC   A0A261SNI3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=CEG14_05255 {ECO:0000313|EMBL:OZI38948.1};
OS   Bordetella genomosp. 1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1395607 {ECO:0000313|EMBL:OZI38948.1, ECO:0000313|Proteomes:UP000217005};
RN   [1] {ECO:0000313|EMBL:OZI38948.1, ECO:0000313|Proteomes:UP000217005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17610 {ECO:0000313|EMBL:OZI38948.1,
RC   ECO:0000313|Proteomes:UP000217005};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) 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:OZI38948.1}.
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DR   EMBL; NEVL01000002; OZI38948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261SNI3; -.
DR   OrthoDB; 9804645at2; -.
DR   Proteomes; UP000217005; 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; cd00075; HATPase; 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; 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   PRINTS; PR00344; BCTRLSENSOR.
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   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   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        224..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          243..294
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          302..504
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          100..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  56166 MW;  1F219F5768B4114F CRC64;
     MTFSPARLVP RSLRARLILL VLGSVLLTQA ATLATVSYFR QKFMEDVAIG YIATTIRTLR
     ASLAQIPAED RADFVRAASQ NQWRLWSRML PAEARLQRLN MPPPDRFMPG AMPPPPPGPP
     RDDDLDDPVE REQRMEAFRR MEAQRRARHP HDDPDDVRRD LRDLVRELNI RLNDGTRVAL
     SRGPRAEVYI SLAPNPASED APLLREWLVI PLERLDPPVS SPLVAFWLGG LGLVLMLAAW
     FSWHITRPLT RLAQAADQLA AGQPQRVEPA GPHETRALGE RFNAMLDALA ESDSVRRTLL
     SGLPHDLKGP LSRMWLRIEM ADDSVLKEGL RKDLQDMQHM VDQFIGFVRG TDPAAYRYAP
     LEMVDWARDR VGAWQSTNTA ITLDAPEDDS LHVQADAVAL GRLLDNLIGN ALHHGAPPID
     VRLARDGNHA VLEVGDHGTG IAAPRRAEAL RPFARLDDAR TRTGNVGLGL ALTEAITRAH
     GGTLELGDHS GGGLLVRITL PLAPTDPA
//
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