SPAA_STRDO
ID SPAA_STRDO Reviewed; 1528 AA.
AC P21979;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Cell surface antigen I/II {ECO:0000303|PubMed:1855987};
DE AltName: Full=Surface protein antigen A {ECO:0000303|PubMed:1855987};
DE Contains:
DE RecName: Full=Cell surface antigen II;
DE Flags: Precursor;
GN Name=spaA {ECO:0000303|PubMed:1855987};
OS Streptococcus downei (Streptococcus sobrinus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1317;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=6715 / Serotype G;
RX PubMed=1855987; DOI=10.1128/iai.59.8.2677-2685.1991;
RA Lapolla R.J., Haron J.A., Kelly C.G., Taylor W.R., Bohart C., Hendricks M.,
RA Pyati J., Graff R.T., Ma J.K.-C., Lehner T.;
RT "Sequence and structural analysis of surface protein antigen I/II (SpaA) of
RT Streptococcus sobrinus.";
RL Infect. Immun. 59:2677-2685(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 423-817.
RX PubMed=1694526; DOI=10.1128/jb.172.7.3988-4001.1990;
RA Goldschmidt R.M., Thoren-Gordon M., Curtiss R. III;
RT "Regions of the Streptococcus sobrinus spaA gene encoding major
RT determinants of antigen I.";
RL J. Bacteriol. 172:3988-4001(1990).
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- MISCELLANEOUS: Immunodominant determinants are located in the C-
CC terminal two-thirds of the SpaA protein.
CC -!- SIMILARITY: Belongs to the antigen I/II family. {ECO:0000305}.
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DR EMBL; X57841; CAA40973.1; -; Genomic_DNA.
DR EMBL; M38210; AAA26977.1; -; Genomic_DNA.
DR AlphaFoldDB; P21979; -.
DR SMR; P21979; -.
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; 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; PF06696; Strep_SA_rep; 2.
DR SUPFAM; SSF74914; SSF74914; 1.
DR TIGRFAMs; TIGR04228; isopep_sspB_C2; 1.
DR PROSITE; PS51965; AG_I_II_AR; 4.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..?
FT /note="Cell surface antigen I/II"
FT /id="PRO_0000005666"
FT CHAIN ?..1506
FT /note="Cell surface antigen II"
FT /id="PRO_0000005667"
FT PROPEP 1507..1528
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005668"
FT REPEAT 161..235
FT /note="Ag I/II A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 236..315
FT /note="Ag I/II A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 316..396
FT /note="Ag I/II A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 397..478
FT /note="Ag I/II A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REGION 50..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1503..1507
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 50..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..890
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..929
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1506
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 427
FT /note="A -> E (in Ref. 2; AAA26977)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="Q -> K (in Ref. 2; AAA26977)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="Q -> K (in Ref. 2; AAA26977)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="A -> S (in Ref. 2; AAA26977)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="A -> S (in Ref. 2; AAA26977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1528 AA; 165573 MW; B235F9CCD92838E0 CRC64;
MLQKCKLEGI IICNEKRLLG AAKVKSGRTL SGALLGTAIL ASGAGQKALA EETSTTSTSG
GDTAVVGTET GNPATNLPDK QDNPSSQAET SQAQARQKTG AMSVDVSTSE LDEAAKSPQE
AGVTVSQDAT VNKGTVEPSD EANQKEPEIK DDYSKQAADI QKATEDYKAS VAANQAETDR
INQEIAAKKA QYEQDLAANK AEVERSLMRM RKPRPIYEAK LAQNQKDLAA IQQANSDSQA
AYAAAKEAYD KEWARVQAAN AAAKKAYEEA LAANTAKNDQ IKAEIEAIQQ RSAKADYEAK
LAQYEKDLAA AQAGNAANEA DYQAKKAAYE QELARVQAAN AAAKQAYEQA LAANSAKNAQ
ITAENEAIQQ NAQAKADYEA KLAQYQKDLA AAQSGNAANE ADYQEKLAAY EKELARVQAA
NAAAKQAYEQ QVQQANAKNA EITEANRAIR ERNAKAKTDY ELKLSKYQEE LAQYKKDLAE
YPAKLQAYQD EQAAIKAALA ELEKHKNEDG NLSEPSAQSL VYDLEPNAQV ALVTDGKLLK
ASALDEAFSH DEKNYNNHLL QPDNLNVTYL EQADDVASSV ELFGNFGDKA GWTTTVSNGA
EVKFASVLLK RGQSATATYT NLKNSYYNGK KISKVVYKYT VDPDSKFQNP TGNVWLGIFT
DPTLGVFASA YTGQNEKDTS IFIKNEFTFY DEDGNPIDFD NALLSVASLN REHNSIEMAK
DYSGTFVKIS GSSIGEKNGM IYATDTLNFK KGEGGSLHTM YTRASEPGSG WDSADAPNSW
YGAGAVRMSG PNNYITLGAT SATNVLSLAE MPQVPGKDNT AGKKPNIWYS LNGKIRAVNV
PKVTKEKPTP PVEPTKPDEP TYEVEKELVD LPVEPKYEPE PTPPSKNPDQ SIPEKPVEPT
YEVEKELEPA PVEPSYEKEP TPPQSTPDQE EPEKPVEPSY QSLPTPPVEP VYETVPGPVS
VPTVRYHYYK LAVQPGVTKE IKNQDDLDID KTLVAKQSTV KFQLKTADLP AGRPETTSFV
LMDPLPSGYQ LNLEATKVAS PGFEASYDAM THTVTFTATA ETLAALNQDL TKAVATIYPT
VVGQVLNDGA TYTNNFTLMV NDAYGIKSNI VRVTTPGKPN DPDNPSNNYI TPHKVNKNEN
GVVIDGKSVL AGTTNYYELT WDLDQYKGDK SAKEIIQKGF FYVDDYPEEA LDLRTDLIKL
TDANGKAVTG VSVADYASLE AAPAAVQDML KKANIIPKGA FQVFTADDPQ AFYDAYVVTG
TDLTIVTPMT VKAEMGKTGG SYENRAYQID FGNGYESNLV VNNVPKINPE KDVTLTMDPA
DSTNVDGQTI ALNQVFNYRL IGGIIPADHA EELFEYSFSD DYDQTGDQYT GQYKAFAKVD
LTLKDGTIIK AGTDLTSYTE AQVDEANGQI VVTFKEDFLR SVSVDSAFQA EVYLQMKRIA
VGTFANTYVN TVNGITYSSN TVRTSTPEPK QPSPVDPKTT TTVVFQPRQG KAYQPAPPAG
AQLPATGDSS NAYLPLLGLV SLTAGFSC
