SSPB_STRGC
ID SSPB_STRGC Reviewed; 1499 AA.
AC A8AUS1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Streptococcal surface protein B;
DE AltName: Full=Adhesin SspB;
DE Flags: Precursor;
GN Name=sspB {ECO:0000303|PubMed:19884334}; OrderedLocusNames=SGO_0211;
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, NOT INDUCED 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, 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) (PubMed:22609749).
CC {ECO:0000269|PubMed:22609749, ECO:0000269|PubMed:9393810}.
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: In the absence of the sspA gene, collagen does not induce
CC sspB (at protein 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. {ECO:0000305}.
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DR EMBL; CP000725; ABV10074.1; -; Genomic_DNA.
DR RefSeq; WP_011999748.1; NC_009785.1.
DR AlphaFoldDB; A8AUS1; -.
DR SMR; A8AUS1; -.
DR STRING; 467705.SGO_0211; -.
DR EnsemblBacteria; ABV10074; ABV10074; SGO_0211.
DR KEGG; sgo:SGO_0211; -.
DR eggNOG; COG3064; Bacteria.
DR eggNOG; COG3087; Bacteria.
DR HOGENOM; CLU_257994_0_0_9; -.
DR OMA; NTITAMM; -.
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..37
FT /evidence="ECO:0000255"
FT CHAIN 38..1499
FT /note="Streptococcal surface protein B"
FT /evidence="ECO:0000255"
FT /id="PRO_5002717041"
FT PROPEP 1470..1499
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_5018359053"
FT REPEAT 145..219
FT /note="Ag I/II A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 220..301
FT /note="Ag I/II A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 302..383
FT /note="Ag I/II A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 384..465
FT /note="Ag I/II A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REGION 50..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1409..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1466..1470
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 50..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..798
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..837
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..876
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1469
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1499 AA; 163982 MW; 7B1954C19D2EC339 CRC64;
MQKREVFGFR KSKVAKTLCG AVLGAALIAI ADQQVLADEV TETNSTANVA VTTTGNPATN
LPEAQGEATE AASQSQAQAG SKDGALPVEV SADDLNKAVT DAKAAGVNVV QDQTSDKGTA
TTAAENAQKQ AEIKSDYAKQ AEEIKKTTEA YKKEVEAHQA ETDKINAENK AAEDKYQEDL
KAHQAEVEKI NTANATAKAE YEAKLAQYQK DLAAVQKANE DSQLDYQNKL SAYQAELARV
QKANAEAKEA YEKAVKENTA KNAALQAENE AIKQRNETAK ANYDAAMKQY EADLAAIKKA
KEDNDADYQA KLAAYQAELA RVQKANADAK AAYEKAVEEN TAKNTAIQAE NEAIKQRNET
AKATYEAAVK QYEADLAAVK QANATNEADY QAKLAAYQTE LARVQKANAD AKATYEKAVE
DNKAKNAALQ AENEEIKQRN AAAKTDYEAK LAKYEADLAK YKKDFAAYTA ALAEAESKKK
QDGYLSEPRS QSLNFKSEPN AIRTIDSSVH QYGQQELDAL VKSWGISPTN PDRKKSTAYS
YFNAINSNNT YAKLVLEKDK PVDVTYTGLK NSSFNGKKIS KVVYTYTLKE TGFNDGTKMT
MFASSDPTVT AWYNDYFTST NINVKVKFYD EEGQLMNLTG GLVNFSSLNR GNGSGAIDKD
AIESVRNFNG RYIPISGSSI KIHENNSAYA DSSNAEKSRG ARWDTSEWDT TSSPNNWYGA
IVGEITQSEI SFNMASSKSG NIWFAFNSNI NAIGVPTKPV APTAPTQPMY ETEKPLEPAP
VVPTYENEPT PPVKTPDQPE PSKPEEPTYE TEKPLEPAPV APTYENEPTP PVKIPDQPEP
SKPEEPTYET EKPLEPAPVA PTYENEPTPP VKTPDQPEPS KPEEPTYDPL PTPPLAPTPK
QLPTPPVVPT VHFHYSSLLA QPQINKEIKN EDGVDIDRTL VAKQSIVKFE LKTEALTAGR
PKTTSFVLVD PLPTGYKFDL DATKAASTGF DTTYDEASHT VTFKATDETL ATYNADLTKP
VETLHPTVVG RVLNDGATYT NNFTLTVNDA YGIKSNVVRV TTPGKPNDPD NPNNNYIKPT
KVNKNKEGLN IDGKEVLAGS TNYYELTWDL DQYKGDKSSK EAIQNGFYYV DDYPEEALDV
RPDLVKVADE KGNQVSGVSV QQYDSLEAAP KKVQDLLKKA NITVKGAFQL FSADNPEEFY
KQYVSTGTSL VITDPMTVKS EFGKTGGKYE NKAYQIDFGN GYATEVVVNN VPKITPKKDV
TVSLDPTSEN LDGQTVQLYQ TFNYRLIGGL IPQNHSEELE DYSFVDDYDQ AGDQYTGNYK
TFSSLNLTMK DGSVIKAGTD LTSQTTAETD ATNGIVTVRF KEDFLQKISL DSPFQAETYL
QMRRIAIGTF ENTYVNTVNK VAYASNTVRT TTPIPRTPDK PTPIPTPKPK DPDKPETPKE
PKVPSPKVED PSAPIPVSVG KELTTLPKTG TNDATYMPYL GLAALVGFLG LGLAKRKED
