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PAC_STRMG
ID   PAC_STRMG               Reviewed;        1565 AA.
AC   P11657;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Major cell-surface adhesin PAc {ECO:0000303|PubMed:2761390};
DE   AltName: Full=Antigen I/II;
DE   Flags: Precursor;
GN   Name=pac {ECO:0000303|PubMed:2761390};
OS   Streptococcus mutans.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 39-48.
RC   STRAIN=MT8148 / Serotype c;
RX   PubMed=2761390; DOI=10.1111/j.1365-2958.1989.tb00215.x;
RA   Okahashi N., Sasakawa C., Yoshikawa M., Hamada S., Koga T.;
RT   "Molecular characterization of a surface protein antigen gene from serotype
RT   c Streptococcus mutans, implicated in dental caries.";
RL   Mol. Microbiol. 3:673-678(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MT8148 / Serotype c;
RA   Terao Y., Kawabata S., Hamada S.;
RT   "Identification of Streptococcus mutans rgtB gene as a regulator of
RT   glucosyltransferase expression.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 463-839.
RC   STRAIN=OMZ175 / Serotype f;
RX   PubMed=12054777; DOI=10.1016/s0022-2836(02)00025-6;
RA   Troffer-Charlier N., Ogier J., Moras D., Cavarelli J.;
RT   "Crystal structure of the V-region of Streptococcus mutans antigen I/II at
RT   2.4 A resolution suggests a sugar preformed binding site.";
RL   J. Mol. Biol. 318:179-188(2002).
CC   -!- FUNCTION: Surface protein antigen implicated in dental caries.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}.
CC   -!- SIMILARITY: Belongs to the antigen I/II family. {ECO:0000305}.
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DR   EMBL; X14490; CAA32652.1; -; Genomic_DNA.
DR   EMBL; AB040534; BAC54564.1; -; Genomic_DNA.
DR   PIR; S04729; S04729.
DR   PDB; 1JMM; X-ray; 2.40 A; A=463-839.
DR   PDB; 3OPU; X-ray; 2.18 A; A/B/C/D/E/F=1154-1492.
DR   PDB; 3QE5; X-ray; 2.50 A; A/B=991-1485.
DR   PDB; 6TZL; X-ray; 1.60 A; A/B/C/D=446-848.
DR   PDB; 6UBV; X-ray; 2.70 A; A/B/C/D=446-848.
DR   PDBsum; 1JMM; -.
DR   PDBsum; 3OPU; -.
DR   PDBsum; 3QE5; -.
DR   PDBsum; 6TZL; -.
DR   PDBsum; 6UBV; -.
DR   AlphaFoldDB; P11657; -.
DR   BMRB; P11657; -.
DR   SMR; P11657; -.
DR   STRING; 1198676.SMUGS5_02680; -.
DR   eggNOG; COG3064; Bacteria.
DR   eggNOG; COG3087; Bacteria.
DR   EvolutionaryTrace; P11657; -.
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; Repeat; Secreted; Signal.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000269|PubMed:2761390"
FT   CHAIN           39..1535
FT                   /note="Major cell-surface adhesin PAc"
FT                   /id="PRO_0000005645"
FT   PROPEP          1536..1565
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000005646"
FT   REPEAT          146..220
FT                   /note="Ag I/II A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT   REPEAT          221..302
FT                   /note="Ag I/II A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT   REPEAT          303..384
FT                   /note="Ag I/II A 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT   REPEAT          385..466
FT                   /note="Ag I/II A 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT   REPEAT          848..887
FT                   /note="P1"
FT   REPEAT          888..926
FT                   /note="P2"
FT   REPEAT          927..964
FT                   /note="P3"
FT   REGION          42..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..448
FT                   /note="Heptad repeats of Y-[EQ]-X-X-L-A-X"
FT   REGION          461..834
FT                   /note="V-region (lectin-like)"
FT   REGION          827..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1486..1511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1532..1536
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        42..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..892
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        900..931
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..983
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1535
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   HELIX           446..454
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           458..490
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           491..493
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          499..502
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          517..527
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           529..536
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           539..541
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           542..545
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   TURN            546..548
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           552..554
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           557..560
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           563..565
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          566..569
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          572..576
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           577..579
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   TURN            585..587
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          593..599
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          604..610
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          624..631
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          638..640
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          642..649
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           650..652
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          654..657
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          664..666
FT                   /evidence="ECO:0007829|PDB:1JMM"
FT   STRAND          668..678
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          687..694
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          703..709
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          711..715
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          721..725
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          728..731
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           741..743
FT                   /evidence="ECO:0007829|PDB:6UBV"
FT   STRAND          751..753
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          759..762
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           766..769
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          771..778
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          780..788
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           789..791
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   HELIX           795..797
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          812..816
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          818..820
FT                   /evidence="ECO:0007829|PDB:6TZL"
FT   STRAND          824..826
FT                   /evidence="ECO:0007829|PDB:1JMM"
FT   STRAND          1003..1009
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1025..1032
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1045..1050
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1055..1057
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   HELIX           1059..1064
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1069..1074
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   HELIX           1075..1077
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1079..1084
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   HELIX           1086..1093
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   TURN            1094..1097
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1106..1111
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1117..1120
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1123..1126
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   TURN            1127..1129
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1130..1133
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1137..1140
FT                   /evidence="ECO:0007829|PDB:3QE5"
FT   STRAND          1159..1161
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1180..1187
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   HELIX           1190..1192
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   HELIX           1199..1202
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1206..1211
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   TURN            1214..1216
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1217..1219
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   HELIX           1221..1223
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1225..1228
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1236..1244
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   TURN            1245..1247
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   HELIX           1250..1258
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1267..1273
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   HELIX           1275..1282
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   TURN            1283..1286
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1289..1297
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   HELIX           1299..1304
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1306..1316
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1319..1330
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1336..1342
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1361..1367
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1373..1377
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1382..1387
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   TURN            1390..1392
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1393..1405
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1407..1409
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   HELIX           1422..1424
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1425..1430
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   TURN            1431..1434
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1435..1440
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   HELIX           1442..1447
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1456..1464
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1466..1472
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1474..1478
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1481..1484
FT                   /evidence="ECO:0007829|PDB:3OPU"
FT   STRAND          1488..1492
FT                   /evidence="ECO:0007829|PDB:3OPU"
SQ   SEQUENCE   1565 AA;  170782 MW;  4C3B05C809D0C32A CRC64;
     MKVKKTYGFR KSKISKTLCG AVLGTVAAVS VAGQKVFADE TTTTSDVDTK VVGTQTGNPA
     TNLPEAQGSA SKEAEQSQTK LERQMVHTIE VPKTDLDQAA KDAKSAGVNV VQDADVNKGT
     VKTPEEAVQK ETEIKEDYTK QAEDIKKTTD QYKSDVAAHE AEVAKIKAKN QATKEQYEKD
     MAAHKAEVER INAANAASKT AYEAKLAQYQ ADLAAVQKTN AANQAAYQKA LAAYQAELKR
     VQEANAAAKA AYDTAVAANN AKNTEIAAAN EEIRKRNATA KAEYETKLAQ YQAELKRVQE
     ANAANEADYQ AKLTAYQTEL ARVQKANADA KATYEAAVAA NNAKNAALTA ENTAIKQRNE
     NAKATYEAAL KQYEADLAAV KKANAANEAD YQAKLTAYQT ELARVQKANA DAKAAYEAAV
     AANNAANAAL TAENTAIKKR NADAKADYEA KLAKYQADLA KYQKDLADYP VKLKAYEDEQ
     TSIKAALAEL EKHKNEDGNL TEPSAQNLVY DLEPNANLSL TTDGKFLKAS AVDDAFSKST
     SKAKYDQKIL QLDDLDITNL EQSNDVASSM ELYGNFGDKA GWSTTVSNNS QVKWGSVLLE
     RGQSATATYT NLQNSYYNGK KISKIVYKYT VDPKSKFQGQ KVWLGIFTDP TLGVFASAYT
     GQVEKNTSIF IKNEFTFYHE DEKPINFDNA LLSVTSLNRE HNSIEMAKDY SGKFVKISGS
     SIGEKNGMIY ATDTLNFKQG EGGSRWTMYK NSQAGSGWDS SDAPNSWYGA GAIKMSGPNN
     HVTVGATSAT NVMPVSDMPV VPGKDNTDGK KPNIWYSLNG KIRAVNVPKV TKEKPTPPVK
     PTAPTKPTYE TEKPLKPAPV APNYEKEPTP PTRTPDQAEP NKPTPPTYET EKPLEPAPVE
     PSYEAEPTPP TRTPDQAEPN KPTPPTYETE KPLEPAPVEP SYEAEPTPPT PTPDQPEPNK
     PVEPTYEVIP TPPTDPVYQD LPTPPSDPTV HFHYFKLAVQ PQVNKEIRNN NDINIDRTLV
     AKQSVVKFQL KTADLPAGRD ETTSFVLVDP LPSGYQFNPE ATKAASPGFD VTYDNATNTV
     TFKATAATLA TFNADLTKSV ATIYPTVVGQ VLNDGATYKN NFTLTVNDAY GIKSNVVRVT
     TPGKPNDPDN PNNNYIKPTK VNKNENGVVI DGKTVLAGST NYYELTWDLD QYKNDRSSAD
     TIQKGFYYVD DYPEEALELR QDLVKITDAN GNEVTGVSVD NYTNLEAAPQ EIRDVLSKAG
     IRPKGAFQIF RADNPREFYD TYVKTGIDLK IVSPMVVKKQ MGQTGGSYEN QAYQIDFGNG
     YASNIVINNV PKINPKKDVT LTLDPADTNN VDGQTIPLNT VFNYRLIGGI IPANHSEELF
     EYNFYDDYDQ TGDHYTGQYK VFAKVDITLK NGVIIKSGTE LTQYTTAEVD TTKGAITIKF
     KEAFLRSVSI DSAFQAESYI QMKRIAVGTF ENTYINTVNG VTYSSNTVKT TTPEDPADPT
     DPQDPSSPRT STVIIYKPQS TAYQPSSVQE TLPNTGVTNN AYMPLLGIIG LVTSFSLLGL
     KAKKD
 
 
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