SPAP_STRMU
ID SPAP_STRMU Reviewed; 1562 AA.
AC P23504;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cell surface antigen I/II;
DE Contains:
DE RecName: Full=Cell surface antigen I;
DE Contains:
DE RecName: Full=Cell surface antigen II;
DE Flags: Precursor;
GN Name=spaP {ECO:0000303|PubMed:2687020}; OrderedLocusNames=SMU_610;
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], PROTEIN SEQUENCE OF 39-45 AND 998-1008,
RP AND PROBABLE SUBCELLULAR LOCATION.
RC STRAIN=NG5 / Serotype c;
RX PubMed=2687020; DOI=10.1016/0014-5793(89)81632-1;
RA Kelly C.G., Evans P., Bergmeier L.A., Lee S.F., Progulske-Fox A.,
RA Harris A.C., Aitken A., Bleiweis A.S., Lehner T.;
RT "Sequence analysis of the cloned streptococcal cell surface antigen I/II.";
RL FEBS Lett. 258:127-132(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NG5 / Serotype c;
RX PubMed=1982405; DOI=10.1016/0003-9969(90)90128-w;
RA Kelly C.G., Evans P., Ma J.K.C., Bergmeier L.A., Taylor W., Brady L.J.,
RA Lee S.F., Bleiweis A.S., Lehner T.;
RT "Sequencing and characterization of the 185 kDa cell surface antigen of
RT Streptococcus mutans.";
RL Arch. Oral Biol. 35:33S-38S(1990).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1084-1189.
RX PubMed=1855988; DOI=10.1128/iai.59.8.2686-2694.1991;
RA Ma J.K.C., Kelly C.G., Munro G., Whiley R.A., Lehner T.;
RT "Conservation of the gene encoding streptococcal antigen I/II in oral
RT streptococci.";
RL Infect. Immun. 59:2686-2694(1991).
RN [5] {ECO:0007744|PDB:5LO2, ECO:0007744|PDB:5LO3, ECO:0007744|PDB:5LO4}
RP STRUCTURE BY NMR OF 452-470, DOMAIN, AND MUTAGENESIS OF 456-TYR--TYR-470
RP AND TYR-470.
RX PubMed=28530710; DOI=10.1038/nchembio.2380;
RA Baker E.G., Williams C., Hudson K.L., Bartlett G.J., Heal J.W.,
RA Porter Goff K.L., Sessions R.B., Crump M.P., Woolfson D.N.;
RT "Engineering protein stability with atomic precision in a monomeric
RT miniprotein.";
RL Nat. Chem. Biol. 13:764-770(2017).
CC -!- FUNCTION: Surface protein antigen implicated in dental caries.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000305|PubMed:2687020}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477}.
CC -!- DOMAIN: A short internal peptide (residues 452-470) has been used as a
CC miniprotein to examine protein folding and stability.
CC {ECO:0000269|PubMed:28530710}.
CC -!- PTM: Detected as a 185 kDa cell surface protein, but also as 2 proteins
CC in S.mutans culture supernatants of about 150 kDa (antigen I) and 50
CC kDa (antigen II); antigen II is only seen after proteolysis. Antigen I
CC and II have the same N-terminus but different C-termini.
CC {ECO:0000269|PubMed:2687020}.
CC -!- SIMILARITY: Belongs to the antigen I/II family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X17390; CAA35253.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58348.1; -; Genomic_DNA.
DR PIR; S06839; S06839.
DR RefSeq; NP_721042.1; NC_004350.2.
DR RefSeq; WP_002352221.1; NC_004350.2.
DR PDB; 5LO2; NMR; -; A=452-470.
DR PDB; 5LO3; NMR; -; A=452-470.
DR PDB; 5LO4; NMR; -; A=452-470.
DR PDBsum; 5LO2; -.
DR PDBsum; 5LO3; -.
DR PDBsum; 5LO4; -.
DR AlphaFoldDB; P23504; -.
DR BMRB; P23504; -.
DR SMR; P23504; -.
DR STRING; 210007.SMU_610; -.
DR PRIDE; P23504; -.
DR EnsemblBacteria; AAN58348; AAN58348; SMU_610.
DR KEGG; smu:SMU_610; -.
DR PATRIC; fig|210007.7.peg.542; -.
DR eggNOG; COG3064; Bacteria.
DR eggNOG; COG3087; Bacteria.
DR HOGENOM; CLU_257994_0_0_9; -.
DR OMA; APNSWYG; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR Gene3D; 2.60.530.10; -; 1.
DR InterPro; IPR026345; Adh_isopep-form_adh_dom.
DR InterPro; IPR041324; AgI/II_N.
DR InterPro; IPR032300; Antigen_C.
DR InterPro; IPR021197; Cross-wall-target_lipo_motif.
DR InterPro; IPR013574; Glucan-bd_C/Surface_Ag-I/II_V.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR036234; SA_I/II_PAC_V_sf.
DR InterPro; IPR009578; Surface_Ag_rpt.
DR Pfam; PF18652; Adhesin_P1_N; 1.
DR Pfam; PF17998; AgI_II_C2; 1.
DR Pfam; PF16364; Antigen_C; 1.
DR Pfam; PF08363; GbpC; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF06696; Strep_SA_rep; 7.
DR SUPFAM; SSF74914; SSF74914; 1.
DR TIGRFAMs; TIGR04228; isopep_sspB_C2; 1.
DR TIGRFAMs; TIGR03726; strep_RK_lipo; 1.
DR PROSITE; PS51965; AG_I_II_AR; 4.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Dental caries; Direct protein sequencing;
KW Peptidoglycan-anchor; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000269|PubMed:2687020"
FT CHAIN 39..?
FT /note="Cell surface antigen I"
FT /id="PRO_0000005663"
FT CHAIN 998..1532
FT /note="Cell surface antigen II"
FT /evidence="ECO:0000269|PubMed:2687020"
FT /id="PRO_0000005664"
FT PROPEP 1533..1562
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005665"
FT REPEAT 147..221
FT /note="Ag I/II A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 222..303
FT /note="Ag I/II A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 304..385
FT /note="Ag I/II A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 386..467
FT /note="Ag I/II A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REGION 42..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 824..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1529..1533
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 42..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..889
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..928
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..973
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1532
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 456..470
FT /note="YQADLAKYQKDLADY->FQADLAKFQKDLADF: Miniprotein is
FT less helical."
FT /evidence="ECO:0000269|PubMed:28530710"
FT MUTAGEN 456..470
FT /note="YQADLAKYQKDLADY->HQADLAKHQKDLADH: Miniprotein is no
FT longer helical."
FT /evidence="ECO:0000269|PubMed:28530710"
FT MUTAGEN 456..470
FT /note="YQADLAKYQKDLADY->WQADLAKWQKDLADW: Miniprotein is as
FT helical as wild-type."
FT /evidence="ECO:0000269|PubMed:28530710"
FT CONFLICT 73
FT /note="E -> Q (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 79..90
FT /note="NQAGETNGSIPV -> TKLERQMVHTI (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="E -> G (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="A -> V (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="A -> S (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="V -> L (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 878
FT /note="N -> K (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="V -> I (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010
FT /note="I -> V (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1069
FT /note="T -> A (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1120
FT /note="T -> S (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1201
FT /note="K -> Q (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1241
FT /note="N -> S (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1307
FT /note="N -> D (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1323
FT /note="I -> V (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1371
FT /note="D -> N (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1406..1410
FT /note="FKDGS -> LKNGV (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1416
FT /note="A -> T (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1429
FT /note="A -> T (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1494
FT /note="T -> A (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1512
FT /note="N -> I (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT CONFLICT 1527
FT /note="E -> K (in Ref. 1; CAA35253)"
FT /evidence="ECO:0000305"
FT HELIX 452..469
FT /evidence="ECO:0000269|PubMed:28530710,
FT ECO:0007829|PDB:5LO3"
SQ SEQUENCE 1562 AA; 169972 MW; 298B244E7A95F5D7 CRC64;
MKVKKTYGFR KSKISKTLCG AVLGTVAAVS VAGQKVFADE TTTTSDVDTK VVGTQTGNPA
TNLPEAQGSA SKEAEQSQNQ AGETNGSIPV EVPKTDLDQA AKDAKSAGVN VVQDADVNKG
TVKTAEEAVQ KETEIKEDYT KQAEDIKKTT DQYKSDVAAH EAEVAKIKAK NQATKEQYEK
DMAAHKAEVE RINAANAASK TAYEAKLAQY QADLAAVQKT NAANQAAYQK ALAAYQAELK
RVQEANAAAK AAYDTAVAAN NAKNTEIAAA NEEIRKRNAT AKAEYETKLA QYQAELKRVQ
EANAANEADY QAKLTAYQTE LARVQKANAD AKAAYEAAVA ANNAKNAALT AENTAIKQRN
ENAKATYEAA LKQYEADLAA VKKANAANEA DYQAKLTAYQ TELARVQKAN ADAKAAYEAA
VAANNAANAA LTAENTAIKK RNADAKADYE AKLAKYQADL AKYQKDLADY PVKLKAYEDE
QASIKAALAE LEKHKNEDGN LTEPSAQNLV YDLEPNANLS LTTDGKFLKA SAVDDAFSKS
TSKAKYDQKI LQLDDLDITN LEQSNDVASS MELYGNFGDK AGWSTTVSNN SQVKWGSVLL
ERGQSATATY TNLQNSYYNG KKISKIVYKY TVDPKSKFQG QKVWLGIFTD PTLGVFASAY
TGQVEKNTSI FIKNEFTFYD EDGKPINFDN ALLSVASLNR ENNSIEMAKD YTGKFVKISG
SSIGEKNGMI YATDTLNFRQ GQGGARWTMY TRASEPGSGW DSSDAPNSWY GAGAIRMSGP
NNSVTLGAIS STLVVPADPT MAIETGKKPN IWYSLNGKIR AVNVPKVTKE KPTPPVKPTA
PTKPTYETEK PLKPAPVAPN YEKEPTPPTR TPDQAEPNKP TPPTYETEKP LEPAPVEPSY
EAEPTPPTRT PDQAEPNKPT PPTYETEKPL EPAPVEPSYE AEPTPPTPTP DQPEPNKPVE
PTYEVIPTPP TDPVYQDLPT PPSVPTVHFH YFKLAVQPQV NKEIRNNNDI NIDRTLVAKQ
SVVKFQLKTA DLPAGRDETT SFVLVDPLPS GYQFNPEATK AASPGFDVTY DNATNTVTFK
ATAATLATFN ADLTKSVATI YPTVVGQVLN DGATYKNNFT LTVNDAYGIK SNVVRVTTPG
KPNDPDNPNN NYIKPTKVNK NENGVVIDGK TVLAGSTNYY ELTWDLDQYK NDRSSADTIQ
KGFYYVDDYP EEALELRQDL VKITDANGNE VTGVSVDNYT NLEAAPQEIR DVLSKAGIRP
KGAFQIFRAD NPREFYDTYV KTGIDLKIVS PMVVKKQMGQ TGGSYENQAY QIDFGNGYAS
NIIINNVPKI NPKKDVTLTL DPADTNNVDG QTIPLNTVFN YRLIGGIIPA DHSEELFEYN
FYDDYDQTGD HYTGQYKVFA KVDITFKDGS IIKSGAELTQ YTTAEVDTAK GAITIKFKEA
FLRSVSIDSA FQAESYIQMK RIAVGTFENT YINTVNGVTY SSNTVKTTTP EDPTDPTDPQ
DPSSPRTSTV INYKPQSTAY QPSSVQETLP NTGVTNNAYM PLLGIIGLVT SFSLLGLKAK
KD
