SENX3_MYCS2
ID SENX3_MYCS2 Reviewed; 384 AA.
AC A0QR01; I7FEW3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Signal-transduction histidine kinase SenX3;
DE EC=2.7.13.3;
GN Name=senX3; OrderedLocusNames=MSMEG_0936, MSMEI_0913;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION IN REGULATION OF PHOSPHATE-DEPENDENT GENE EXPRESSION.
RX PubMed=17526710; DOI=10.1128/jb.00190-07;
RA Glover R.T., Kriakov J., Garforth S.J., Baughn A.D., Jacobs W.R. Jr.;
RT "The two-component regulatory system senX3-regX3 regulates phosphate-
RT dependent gene expression in Mycobacterium smegmatis.";
RL J. Bacteriol. 189:5495-5503(2007).
RN [5]
RP REGULATION OF PHNDCE OPERON, AND INDUCTION.
RX PubMed=18083811; DOI=10.1128/jb.01764-07;
RA Gebhard S., Cook G.M.;
RT "Differential regulation of high-affinity phosphate transport systems of
RT Mycobacterium smegmatis: identification of PhnF, a repressor of the phnDCE
RT operon.";
RL J. Bacteriol. 190:1335-1343(2008).
CC -!- FUNCTION: Part of the two-component regulatory system SenX3/RegX3.
CC Phosphorylates RegX3 under conditions of phosphate limitation. Probably
CC does not itself sense phosphate concentrations, which may be relayed to
CC SenX3 by the PstSCAB phosphate transporter system.
CC {ECO:0000269|PubMed:17526710}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By phosphate-limiting growth conditions.
CC {ECO:0000269|PubMed:18083811}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP37393.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK74063.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37393.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011727297.1; NC_018289.1.
DR RefSeq; YP_885339.1; NC_008596.1.
DR AlphaFoldDB; A0QR01; -.
DR SMR; A0QR01; -.
DR STRING; 246196.MSMEI_0913; -.
DR PRIDE; A0QR01; -.
DR EnsemblBacteria; ABK74063; ABK74063; MSMEG_0936.
DR EnsemblBacteria; AFP37393; AFP37393; MSMEI_0913.
DR KEGG; msg:MSMEI_0913; -.
DR KEGG; msm:MSMEG_0936; -.
DR PATRIC; fig|246196.19.peg.926; -.
DR eggNOG; COG5002; Bacteria.
DR OMA; SEHARME; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
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 Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..384
FT /note="Signal-transduction histidine kinase SenX3"
FT /id="PRO_0000357472"
FT DOMAIN 153..369
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 360..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 384 AA; 41862 MW; DFE8034CA4086F24 CRC64;
MSLLTLIAGV AVGVTVVPRI VARRQRRAAY AAGMTVSQML QHITSLSPMG VAVVDTFNDV
VYSNDRAVEL NVVRDRILDD RAWQAAQRVF ETGQDVEVDL SPLKVANPGR SGISVRGKVR
LLTDDDRRFA VVYIDDQSEH ARMEATRRDF VANVSHELKT PVGAMSVLAE ALLASADDPD
TVRRFAEKMV AESHRLADMI GELIELSRLQ GAERLPDLDA VDVDSIVSEA VSRHKVAADN
SQISITTDAP TGYRVLGDEG LLVTAIANLV SNAIAYSPNG TDVSISRRKR GGNIEIAVTD
RGIGIAKDDQ ERVFERFFRV DKARSRATGG TGLGLAIVKH VAANHNGSIR LWSQPGTGST
FTLSIPEYPD PESHSDERED QRER
