ID Y988_STRMU Reviewed; 461 AA.
AC P34001;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Uncharacterized protein SMU_988;
GN OrderedLocusNames=SMU_988;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-373.
RX PubMed=2761387; DOI=10.1111/j.1365-2958.1989.tb00193.x;
RA Ferretti J.J., Russell R.R.B., Dao M.L.;
RT "Sequence analysis of the wall-associated protein precursor of
RT Streptococcus mutans antigen A.";
RL Mol. Microbiol. 3:469-478(1989).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000305}.
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DR EMBL; AE014133; AAN58689.1; -; Genomic_DNA.
DR EMBL; M37842; AAA88609.1; -; Genomic_DNA.
DR PIR; S06993; S06993.
DR RefSeq; NP_721383.1; NC_004350.2.
DR AlphaFoldDB; P34001; -.
DR SMR; P34001; -.
DR STRING; 210007.SMU_988; -.
DR DNASU; 1028330; -.
DR KEGG; smu:SMU_988; -.
DR PATRIC; fig|210007.7.peg.881; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_2_9; -.
DR OrthoDB; 9762009at2; -.
DR PhylomeDB; P34001; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR CDD; cd09154; PLDc_SMU_988_like_1; 1.
DR CDD; cd09160; PLDc_SMU_988_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR NCBIfam; TIGR04265; bac_cardiolipin; 1.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..461
FT /note="Uncharacterized protein SMU_988"
FT /id="PRO_0000201282"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 197..224
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 374..401
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
SQ SEQUENCE 461 AA; 53407 MW; 06973B61D90DAEAF CRC64;
MIGSVLYLVN SQMDTLSIIT WLLVILPFPI LGTLFLIYTK QDWGYRELKS LIKKSTQAIK
PYFQYDQRIL YKLKESHART YNLAQYLHRS GGFPVYKNTK VTYFPNGQSK FEEMKKQLLK
AEKFIFLEYF IIAEGLMWGE ILSILEQKVQ EGVEVRVMYD GMLELSTLSF DYAKRLEKIG
IKAKVFSPIT PFVSTYYNYR DHRKILVIDN KVAFNGGINL ADEYINQIER FGYWKDTAVM
LEGEGVASFT LMFLQMWSTT NKDYEFAPYL TQNFHEIVAN GYVIPYSDSP LDHEKVGENV
YIDILNQARD YVYIMTPYLI LDSEMEHALQ FAAERGVDVK IIMPGIPDKK VPFALAKRYF
PALLDAGVKI YEFTPGFVHA KVFIADDIKA VVGTINLDYR SLYHHFECAT YMYQTDCLVD
IKADFKETLK QSRRVTRSTL QKEKISTKLI GLVVKLVAPL L
//
