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 14-DEC-2022, entry version 86. 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}. 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; 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_I_II_A_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; V-region of surface antigen I/II (SA I/II, PAC); 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 //