SSPA_STRGC
ID SSPA_STRGC Reviewed; 1575 AA.
AC A8AUS0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Streptococcal surface protein A;
DE AltName: Full=Adhesin SspS;
DE Flags: Precursor;
GN Name=sspA {ECO:0000303|PubMed:9393810}; OrderedLocusNames=SGO_0210;
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=17720781; DOI=10.1128/jb.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
RN [2]
RP S.GORDONII IN INFECTIVE ENDOCARDITIS.
RX PubMed=8366515; DOI=10.1099/00222615-39-3-179;
RA Douglas C.W., Heath J., Hampton K.K., Preston F.E.;
RT "Identity of viridans streptococci isolated from cases of infective
RT endocarditis.";
RL J. Med. Microbiol. 39:179-182(1993).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY COLLAGEN, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=9393810; DOI=10.1128/iai.65.12.5157-5164.1997;
RA Love R.M., McMillan M.D., Jenkinson H.F.;
RT "Invasion of dentinal tubules by oral streptococci is associated with
RT collagen recognition mediated by the antigen I/II family of polypeptides.";
RL Infect. Immun. 65:5157-5164(1997).
RN [4]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=19884334; DOI=10.1128/iai.00664-09;
RA Petersen H.J., Keane C., Jenkinson H.F., Vickerman M.M., Jesionowski A.,
RA Waterhouse J.C., Cox D., Kerrigan S.W.;
RT "Human platelets recognize a novel surface protein, PadA, on Streptococcus
RT gordonii through a unique interaction involving fibrinogen receptor
RT GPIIbIIIa.";
RL Infect. Immun. 78:413-422(2010).
RN [5]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=22609749; DOI=10.1099/mic.0.058073-0;
RA Andrian E., Qi G., Wang J., Halperin S.A., Lee S.F.;
RT "Role of surface proteins SspA and SspB of Streptococcus gordonii in innate
RT immunity.";
RL Microbiology 158:2099-2106(2012).
CC -!- FUNCTION: Adhesin that mediates binding of bacteria to a variety of
CC host cells. Plays a role in the bacterial invasion of dentinal tubules
CC (PubMed:9393810). A host immunostimulatory component, it modulates the
CC innate immunity response. Plays a protective role against some
CC antibiotics and cationic antimicrobial peptides (histatin-5, HTN3, but
CC not beta-defensin 4A, DEFB4A). Purified soluble protein stimulates
CC human epithelial cells to produce IL-6 and monocyte chemotactic protein
CC (MCP-1, CCL2) probably via interaction with integrin beta-1 (ITGB1)
CC (PubMed:22609749). {ECO:0000269|PubMed:22609749,
CC ECO:0000269|PubMed:9393810}.
CC -!- SUBUNIT: Binds to human integrin beta-1 (ITGB1).
CC {ECO:0000269|PubMed:22609749}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000269|PubMed:19884334,
CC ECO:0000305|PubMed:9393810}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}. Cell surface {ECO:0000269|PubMed:9393810};
CC Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}.
CC -!- INDUCTION: Induced by growth in the presence of collagen (at protein
CC level). {ECO:0000269|PubMed:9393810}.
CC -!- DISRUPTION PHENOTYPE: Single sspA deletion, bacteria invade human
CC dental roots less well, adhere less well to collagen, decreased
CC accumulation of mature SspB; double sspA-sspB deletion, no invasion of
CC dental roots, collagen adherence is further reduced, as is chaining on
CC soluble collagen (PubMed:9393810). Triple sspA-sspB-hsa deletion no
CC longer causes human platelet aggregation; double sspA-sspB deletion
CC still causes platelet aggregation (PubMed:19884334). Double sspA-sspB
CC adheres better to human epithelial cells and is internalized better
CC than wild-type cells, but induces less host cytokine production (IL-6,
CC IL-8, monocyte chemotactic protein). Stimulates less cytokine
CC production in mouse bone marrow-derived dendritic cells (IL-6, IL-10,
CC IL-12, tumor necrosis factor). Increased sensitivity to antibiotics
CC polymyxin B and nisin, and human histatin-5 (His3-(20-43)-peptide,
CC HTN3). In intranasal mouse infection, the double mutant is cleared less
CC quickly from lungs, neutrophil, hemokine and cytokine production are
CC delayed or reduced (PubMed:22609749). {ECO:0000269|PubMed:19884334,
CC ECO:0000269|PubMed:22609749, ECO:0000269|PubMed:9393810}.
CC -!- MISCELLANEOUS: S.gordonii, a commensal oral cavity bacteria, is among
CC the bacteria most frequently identified as being the primary
CC etiological agents of subacute infective endocarditis (found in 13% of
CC cases). {ECO:0000269|PubMed:8366515}.
CC -!- SIMILARITY: Belongs to the antigen I/II family.
CC {ECO:0000305|PubMed:9393810}.
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DR EMBL; CP000725; ABV10916.1; -; Genomic_DNA.
DR RefSeq; WP_011999747.1; NC_009785.1.
DR AlphaFoldDB; A8AUS0; -.
DR SMR; A8AUS0; -.
DR STRING; 467705.SGO_0210; -.
DR EnsemblBacteria; ABV10916; ABV10916; SGO_0210.
DR KEGG; sgo:SGO_0210; -.
DR eggNOG; COG3064; Bacteria.
DR eggNOG; COG3087; Bacteria.
DR HOGENOM; CLU_257994_0_0_9; -.
DR OMA; APNSWYG; -.
DR Proteomes; UP000001131; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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; 5.
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 Cell wall; Dental caries; Peptidoglycan-anchor; Reference proteome; Repeat;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..1575
FT /note="Streptococcal surface protein A"
FT /evidence="ECO:0000255"
FT /id="PRO_5002717652"
FT PROPEP 1543..1575
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_5018350862"
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 REGION 52..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1539..1543
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 52..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..910
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..949
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..978
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1542
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1575 AA; 171926 MW; 5F9EA5F22CC2278D CRC64;
MNKRKEVFGF RKSKVAKTLC GAVLGAALIA IADQQVLADE VTETNSTANV AVTTTGNPAT
NLPEAQGEAT EAASQSQAQA GSKEGALPVE VSADDLNQAV TDAKAAGVNV VQDQTSDKGT
ATTAAENAQK QAEIKSDYAK QAEEIKKTTE AYKKEVEAHQ AETDKINAEN KAAEDKYQED
LKAHQAEVEK INTANATAKA EYEAKLAQYQ KDLAAVQKAN EDSQLDYQNK LSAYQAELAR
VQKANAEAKE AYEKAVKENT AKNAALQAEN EAIKQRNETA KANYDAAMKQ YEADLAAIKK
AKEDNDADYQ AKLAAYQAEL ARVQKANADA KAAYEKAVEE NTAKNTAIQA ENEAIKQRNA
AAKATYEAAL KQYEADLAAA KKANEDSDAD YQAKLAAYQT ELARVQKANA DAKAAYEKAV
EDNKAKNAAL QAENEEIKQR NAAAKTDYEA KLAKYEADLA KYKKELAEYP AKLKAYEDEQ
AQIKAALVEL EKNKNQDGYL SKPSAQSLVY DSEPNAQLSL TTNGKMLKAS AVDEAFSHDT
AQYSKKILQP DNLNVSYLQQ ADDVTSSMEL YGNFGDKAGW TTTVGNNTEV KFASVLLERG
QSVTATYTNL EKSYYNGKKI SKVVFKYTLD SDSKFKNVDK AWLGVFTDPT LGVFASAYTG
QEEKDTSIFI KNEFTFYDEN DQPINFDNAL LSVASLNREN NSIEMAKDYS GTFVKISGSS
VGEKDGKIYA TETLNFKQGQ GGSRWTMYKN SQPGSGWDSS DAPNSWYGAG AISMSGPTNH
VTVGAISATQ VVPSDPVMAV ATGKRPNIWY SLNGKIRAVN VPKITKEKPT PPVAPTEPQA
PTYEVEKPLE PAPVAPTYEN EPTPPVKTPD QPEPSKPEEP TYETEKPLEP APVVPTYENE
PTPPVKTPDQ PEPSKPEEPT YETEKPLEPA PVAPTYENEP TPPVKTPDQP EPSKPEEPTY
DPLPTPPVAP TPKQLPTPPV VPTVHFHYSS LLAQPQINKE IKNEDGVDID RTLVAKQSIV
KFELKTEALT AGRPKTTSFV LVDPLPTGYK FDLDATKAAS TGFDTTYDEA SHTVTFKATD
ETLATYNADL TKPVETLHPT VVGRVLNDGA TYTNNFTLTV NDAYGIKSNV VRVTTPGKPN
DPDNPNNNYI KPTKVNKNKE GLNIDGKEVL AGSTNYYELT WDLDQYKGDK SSKEAIQNGF
YYVDDYPEEA LDVRPDLVKV ADEKGNQVSG VSVQQYDSLE AAPKKVQDLL KKANITVKGA
FQLFSADNPE EFYKQYVSTG TSLVITDPMT VKSEFGKTGG KYENKAYQID FGNGYATEVV
VNNVPKITPK KDVTVSLDPT SENLDGQTVQ LYQTFNYRLI GGLIPQNHSE ELEDYSFVDD
YDQAGDQYTG NYKTFSSLNL TMKDGSVIKA GTDLTSQTTA ETDAANGIVT VRFKEDFLQK
ISLDSPFQAE TYLQMRRIAI GTFENTYVNT VNKVAYASNT VRTTTPIPRT PDKPTPIPTP
KPKDPDKPET PKEPKVPSPK VEDPSAPIPV SVGKELTTLP KTGTNDSSYM PYLGLAALVG
VLGLGQLKRK EDESN
