ID A8R5F8_STRMG Unreviewed; 1566 AA.
AC A8R5F8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=PA {ECO:0000313|EMBL:BAF91900.1};
GN Name=pa {ECO:0000313|EMBL:BAF91900.1};
OS Streptococcus mutans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1309 {ECO:0000313|EMBL:BAF91900.1};
RN [1] {ECO:0000313|EMBL:BAF91900.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NN2115 {ECO:0000313|EMBL:BAF91900.1};
RA Nakano K., Nomura R., Ooshima T.;
RT "Characterization of protein antigen in serotype k Streptococcus mutans
RT cinical isolates.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the antigen I/II family.
CC {ECO:0000256|ARBA:ARBA00024351, ECO:0000256|PROSITE-ProRule:PRU01310}.
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DR EMBL; AB364278; BAF91900.1; -; Genomic_DNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.740; -; 3.
DR Gene3D; 6.10.250.2200; -; 4.
DR Gene3D; 2.60.530.10; Major cell-surface adhesin PAc; 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_I_II_A_rpt.
DR NCBIfam; TIGR04228; isopep_sspB_C2; 1.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; NF033804; Streccoc_I_II; 1.
DR NCBIfam; TIGR03726; strep_RK_lipo; 1.
DR PANTHER; PTHR10013; GENERAL VESICULAR TRANSPORT FACTOR P115; 1.
DR PANTHER; PTHR10013:SF0; GENERAL VESICULAR TRANSPORT FACTOR P115; 1.
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 PRINTS; PR01217; PRICHEXTENSN.
DR SUPFAM; SSF74914; V-region of surface antigen I/II (SA I/II, PAC); 1.
DR PROSITE; PS51965; AG_I_II_AR; 4.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..1566
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002728394"
FT TRANSMEM 1542..1561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 147..221
FT /note="Ag I/II A"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01310"
FT REPEAT 222..303
FT /note="Ag I/II A"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01310"
FT REPEAT 304..385
FT /note="Ag I/II A"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01310"
FT REPEAT 386..467
FT /note="Ag I/II A"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01310"
FT DOMAIN 1533..1566
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 42..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1486..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..497
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 42..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..893
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..932
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..974
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1566 AA; 170432 MW; B64F83F3FFD3DC53 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
EANVANEADY 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 EHNSIEMAKD YSGKFVKISG
SSIGEKNGMI YATDTLNFKQ GEGGSRWTMY KNSQAGSGWD SSDAPNSWYG AGAIKMSGPN
NHVTVGATSA TNVMPVSDMP VVPGKDNTDG KKPNIWYSLN GKIRAVNVPK VTKEKPTPPV
KPTAPTKPTY ETEKPLKPAP VAPNYEKEPT PPTRTPDQAE PNKPTPPTYE TEKPLEPAPV
EPSYEAEPTP PTRTPDQAEP NKPTPPTYET EKPLEPAPVE PSYEAEPTPP TPTPDQPEPN
KPVEPTYEVI PTPPTDPVYQ DLPTPPSVPT VHFHYFKLAV QPQVNKEIRN NNDVNIDRTL
VAKQSVVKFQ LKTADLPAGR DETTSFVLVD PLPSGYQFNP EATKAASPGF DVAYDDATNT
VTFKATAATL ATFNADLTKS VATIYPTVVG QVLNDGATYK NNFTLTVNDA YGIKSNVVRV
TTPGKPNDPD NPNNNYIKPT KVNKNENGVV IDGKTVLAGS TNYYELTWDL DQYKNDRSSA
DTIQKGFYYV DDYPEEALEL RQDLVKITDA NGNEVTGVSV DNYTSLEAAP QEIRDVLSKA
GIRPKGAFQI FRANNPREFY DTYVKTGIDL KIVSPMVVKK QMGQTGGSYE NQAYQIDFGN
GYASNIIINN VPKINPKKDV TLTLDPADTN NVDGQTIPLN TVFNYRLIGG IIPANHSEEL
FEYNFYDDYD QTGDHYTGHY KVFAKVDITF KDGSIIKSGT ELTQYTTAEV DTTKGAITIK
FKEAFLRSVS IDSVFQAESY IQMKRIAVGT FENTYINTVN GVTYSSNTVK TTTPEDPTDP
TDPQDPASPR TSTVINYKPQ STAYQPSSVQ KTLPNTGVTN NAYMPLLGII GLVTSFSLLG
LKAKKD
//
