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Database: UniProt
Entry: Q1WCR4_STRTR
LinkDB: Q1WCR4_STRTR
Original site: Q1WCR4_STRTR 
ID   Q1WCR4_STRTR            Unreviewed;       468 AA.
AC   Q1WCR4;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   SubName: Full=Eps7A {ECO:0000313|EMBL:ABD96544.1};
GN   Name=epsA {ECO:0000313|EMBL:ABD96544.1};
OS   Streptococcus thermophilus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308 {ECO:0000313|EMBL:ABD96544.1};
RN   [1] {ECO:0000313|EMBL:ABD96544.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EU20 {ECO:0000313|EMBL:ABD96544.1};
RA   de Vin F., Herman L., De Vuyst L.;
RT   "Biodiversity of eps gene clusters and their glycosyltransferases in
RT   Streptococcus thermophilus.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABD96544.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EU20 {ECO:0000313|EMBL:ABD96544.1};
RA   De Vuyst L., Weckx S., Ravyts F., Herman L., Leroy F.;
RT   "New insights into the exopolysaccharide production of Streptococcus
RT   thermophilus.";
RL   Int. Dairy J. 21:586-591(2011).
CC   -!- SIMILARITY: Belongs to the LytR/CpsA/Psr (LCP) family.
CC       {ECO:0000256|ARBA:ARBA00006068}.
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DR   EMBL; DQ393660; ABD96544.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1WCR4; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   Gene3D; 3.40.630.190; LCP protein; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR   InterPro; IPR004190; DNA_pol_proc_fac.
DR   InterPro; IPR004474; LytR_CpsA_psr.
DR   NCBIfam; TIGR00350; lytR_cpsA_psr; 1.
DR   PANTHER; PTHR33392; POLYISOPRENYL-TEICHOIC ACID--PEPTIDOGLYCAN TEICHOIC ACID TRANSFERASE TAGU; 1.
DR   PANTHER; PTHR33392:SF6; POLYISOPRENYL-TEICHOIC ACID--PEPTIDOGLYCAN TEICHOIC ACID TRANSFERASE TAGU; 1.
DR   Pfam; PF02916; DNA_PPF; 1.
DR   Pfam; PF03816; LytR_cpsA_psr; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        31..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          54..169
FT                   /note="DNA polymerase processivity factor"
FT                   /evidence="ECO:0000259|Pfam:PF02916"
FT   DOMAIN          230..376
FT                   /note="Cell envelope-related transcriptional attenuator"
FT                   /evidence="ECO:0000259|Pfam:PF03816"
SQ   SEQUENCE   468 AA;  51353 MW;  39FE9EB83FD185CD CRC64;
     MVNVGLTILY AILALVLLFT MFNYNFLSFR FLNIIITIGL LVVLAISIFL QKTKKSPLVT
     TVVLVIFSLV SLVGIFGFKQ MIDITNRMNQ TAAFSEVEMS IVVPKESDIK DVSQLTSVQA
     PTKVDKNNIE TLMSALKKDK KVDVKVDDVA SYQEAYDNLK SGKSKAMVLS GSYASLLESV
     DSNYASNLKT IYTYKIKKKN NNSAKQVDSK VFNIYISGID TYGSISTVSR SDVNIIMTVN
     MNTHKILLTT TPRDAYVKIP GGGANQYDKL THAGIYGVET SEQTLENLYG IKIDYYARIN
     FTSFLKLIDQ LGGVTVHNDQ AFTSLHGKFD FPVGDIQMNS EQALGFVRER YSLDGGDNDR
     GKNQEKVISA IVNKLASLKS VSNFTSIVNN LQDSVQTNIS LDTINALANT QLDSGSKFTV
     TSQAVTGTGS TGQLTSYAMP NSSLYMMKLD NSSVASASQA IKNLMEEK
//
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