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Database: UniProt
Entry: A0A0H3C621_CAUVN
LinkDB: A0A0H3C621_CAUVN
Original site: A0A0H3C621_CAUVN 
ID   A0A0H3C621_CAUVN        Unreviewed;       475 AA.
AC   A0A0H3C621;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
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   OrderedLocusNames=CCNA_01239 {ECO:0000313|EMBL:ACL94704.1};
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL94704.1, ECO:0000313|Proteomes:UP000001364};
RN   [1] {ECO:0000313|EMBL:ACL94704.1, ECO:0000313|Proteomes:UP000001364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX   PubMed=20472802; DOI=10.1128/JB.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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};
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DR   EMBL; CP001340; ACL94704.1; -; Genomic_DNA.
DR   RefSeq; WP_010919065.1; NC_011916.1.
DR   RefSeq; YP_002516612.1; NC_011916.1.
DR   AlphaFoldDB; A0A0H3C621; -.
DR   SMR; A0A0H3C621; -.
DR   GeneID; 7333632; -.
DR   KEGG; ccs:CCNA_01239; -.
DR   PATRIC; fig|565050.3.peg.1221; -.
DR   HOGENOM; CLU_000445_89_27_5; -.
DR   OrthoDB; 9804645at2; -.
DR   PhylomeDB; A0A0H3C621; -.
DR   Proteomes; UP000001364; Chromosome.
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   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   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, ECO:0000313|EMBL:ACL94704.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001364};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACL94704.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          219..271
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          279..475
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          114..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  51395 MW;  5178BCAF86706349 CRC64;
     MILSRRGAPL FVQALELVIV TLVAAQLISI AVIFTLPPPP PEFYRSSEIV RALKTGQPVQ
     PRDGRLLVVK QDGSIRAGNP ETPRRADFKA GIGKALGVPA NRVELQIDNG PRFFVRRTPV
     TPPRPDAPPA GANGRPGARE PFAREGGAPG GGDNARSAQA RDEPLIFGDF KVGVRQSDGR
     WLVVEPKPTL RFDSWQQRIL LILLLSVIAV TPLAWLFARR LAQPITAFAD AAERLGKDPR
     TPPLNMTGSG EVVAAASAFN MMQERLRRYV EDRTAMVGAI AHDLRTPLTR LKFRIEAAPE
     DIRPKLAADI DQMEAMISAT LGFVRDTNRP AERTKLELSS LLESVMDEAA ETGGDATVER
     SEKTVIEGDP VALKRLVSNL VENALKYGGR ARGRVFSEDG MAIIEIDDDG PGVPPAELER
     VFEPFYRGEP SRNRETGGIG LGLAVVRSLA RAHGGDVVLA NRLGGGLRAT VKLPA
//
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