WAPA_STRMU
ID WAPA_STRMU Reviewed; 453 AA.
AC P11000;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Wall-associated protein;
DE Flags: Precursor;
GN Name=wapA; OrderedLocusNames=SMU_987;
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].
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).
RN [2]
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 -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
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DR EMBL; M37842; AAA88608.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58688.1; -; Genomic_DNA.
DR PIR; S06992; S06992.
DR RefSeq; NP_721382.1; NC_004350.2.
DR RefSeq; WP_002262850.1; NC_004350.2.
DR AlphaFoldDB; P11000; -.
DR SMR; P11000; -.
DR STRING; 210007.SMU_987; -.
DR PRIDE; P11000; -.
DR EnsemblBacteria; AAN58688; AAN58688; SMU_987.
DR KEGG; smu:SMU_987; -.
DR PATRIC; fig|210007.7.peg.880; -.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_002287_5_0_9; -.
DR OMA; HWKVLIN; -.
DR PhylomeDB; P11000; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.1280; -; 1.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR008456; Collagen-bd_dom.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR041171; SDR_Ig.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF05737; Collagen_bind; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall; Peptidoglycan-anchor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT CHAIN 30..425
FT /note="Wall-associated protein"
FT /id="PRO_0000005673"
FT PROPEP 426..453
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005674"
FT REGION 331..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 422..426
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 337..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 425
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 353..360
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 48900 MW; FA13C4C39629A2D2 CRC64;
MKMKRKLLSL VSVLTILLGA FWVTKIVKAD QVTNYTNTAS ITKSDGTALS NDPSKAVNYW
EPLSFSNSIT FPDEVSIKAG DTLTIKLPEQ LQFTTALTFD VMHTNGQLAG KATTDPNTGE
VTVTFTDIFE KLPNDKAMTL NFNAQLNHNN ISIPGVVNFN YNNVAYSSYV KDKDITPISP
DVNKVGYQDK SNPGLIHWKV LINNKQGAID NLTLTDVVGE DQEIVKDSLV AARLQYIAGD
DVDSLDEAAS RPYAEDFSKN VTYQTNDLGL TTGFTYTIPG SSNNAIFISY TTRLTSSQSA
GKDVSNTIAI SGNNINYSNQ TGYARIESAY GRASSRVKRQ AETTTVTETT TSSSSETTTS
EATTETSSTT NNNSTTTETA TSTTGASTTQ TKTTASQTNV PTTTNITTTS KQVTKQKAKF
VLPSTGEQAG LLLTTVGLVI VAVAGVYFYR TRR