Y1061_STRMU
ID Y1061_STRMU Reviewed; 110 AA.
AC P96468; Q54432;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=UPF0122 protein SMU_1061;
GN Name=ylxM; OrderedLocusNames=SMU_1061;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JH1005;
RX PubMed=8763945; DOI=10.1128/jb.178.14.4166-4175.1996;
RA Gutierrez J.A., Crowley P.J., Brown D.P., Hillman J.D., Youngman P.,
RA Bleiweis A.S.;
RT "Insertional mutagenesis and recovery of interrupted genes of Streptococcus
RT mutans by using transposon Tn917: preliminary characterization of mutants
RT displaying acid sensitivity and nutritional requirements.";
RL J. Bacteriol. 178:4166-4175(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JH1005;
RA Gutierrez J.A., Cvitkovitch D.G., Brady L.J., Hamilton I.R., Hillman J.D.,
RA Bleiweis A.S.;
RT "Ffh of Streptococcus mutans is involved in acidurance.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: Might take part in the signal recognition particle (SRP)
CC pathway. This is inferred from the conservation of its genetic
CC proximity to ftsY/ffh. May be a regulatory protein.
CC -!- SIMILARITY: Belongs to the UPF0122 family. {ECO:0000305}.
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DR EMBL; U48884; AAC44501.1; -; Genomic_DNA.
DR EMBL; U88582; AAB48049.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58759.1; -; Genomic_DNA.
DR RefSeq; NP_721453.1; NC_004350.2.
DR RefSeq; WP_002262279.1; NC_004350.2.
DR AlphaFoldDB; P96468; -.
DR SMR; P96468; -.
DR STRING; 210007.SMU_1061; -.
DR PRIDE; P96468; -.
DR EnsemblBacteria; AAN58759; AAN58759; SMU_1061.
DR GeneID; 66817536; -.
DR KEGG; smu:SMU_1061; -.
DR PATRIC; fig|210007.7.peg.948; -.
DR eggNOG; COG2739; Bacteria.
DR HOGENOM; CLU_129218_1_0_9; -.
DR OMA; SIQEWQE; -.
DR PhylomeDB; P96468; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0030695; F:GTPase regulator activity; IMP:CACAO.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00245; UPF0122; 1.
DR InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR InterPro; IPR007394; UPF0122.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR40083; PTHR40083; 1.
DR Pfam; PF04297; UPF0122; 1.
DR SUPFAM; SSF88659; SSF88659; 1.
PE 3: Inferred from homology;
KW Reference proteome.
FT CHAIN 1..110
FT /note="UPF0122 protein SMU_1061"
FT /id="PRO_0000211885"
FT CONFLICT 75
FT /note="D -> A (in Ref. 1; AAC44501)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="T -> S (in Ref. 1; AAC44501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 13252 MW; A816F07684C9EF9F CRC64;
MEIEKTNRMN ALFEFYAALL TDKQMNYIEL YYADDYSLAE IAEEFDVSRQ AVYDNIKRTE
KILEDYEMKL HMYSDYVVRS EIFDAIMKKY PNDPYLQNKI SILTTIDNRD