HSA_STRGC
ID HSA_STRGC Reviewed; 2178 AA.
AC A8AWU7; Q9KWR3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Streptococcal hemagglutinin {ECO:0000303|PubMed:11854202};
DE AltName: Full=Hs antigen {ECO:0000303|PubMed:11854202};
DE AltName: Full=Sialic acid-binding adhesin {ECO:0000303|PubMed:15213130};
DE Flags: Precursor;
GN Name=hsa {ECO:0000303|PubMed:11854202}; OrderedLocusNames=SGO_0966;
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 [GENOMIC DNA], FUNCTION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=11854202; DOI=10.1128/iai.70.3.1209-1218.2002;
RA Takahashi Y., Konishi K., Cisar J.O., Yoshikawa M.;
RT "Identification and characterization of hsa, the gene encoding the sialic
RT acid-binding adhesin of Streptococcus gordonii DL1.";
RL Infect. Immun. 70:1209-1218(2002).
RN [2]
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 [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, GLYCOSLYATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=15213130; DOI=10.1128/iai.72.7.3876-3882.2004;
RA Takahashi Y., Yajima A., Cisar J.O., Konishi K.;
RT "Functional analysis of the Streptococcus gordonii DL1 sialic acid-binding
RT adhesin and its essential role in bacterial binding to platelets.";
RL Infect. Immun. 72:3876-3882(2004).
RN [5]
RP FUNCTION, 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 [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=21071690; DOI=10.1161/atvbaha.110.216515;
RA Keane C., Petersen H., Reynolds K., Newman D.K., Cox D., Jenkinson H.F.,
RA Newman P.J., Kerrigan S.W.;
RT "Mechanism of outside-in {alpha}IIb{beta}3-mediated activation of human
RT platelets by the colonizing Bacterium, Streptococcus gordonii.";
RL Arterioscler. Thromb. Vasc. Biol. 30:2408-2415(2010).
RN [7]
RP FUNCTION IN ADHERENCE TO HOST CELLS AND BIOFILM FORMATION, GLYCOSLYATION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=27616700; DOI=10.1111/cmi.12667;
RA Haworth J.A., Jenkinson H.F., Petersen H.J., Back C.R., Brittan J.L.,
RA Kerrigan S.W., Nobbs A.H.;
RT "Concerted functions of Streptococcus gordonii surface proteins PadA and
RT Hsa mediate activation of human platelets and interactions with
RT extracellular matrix.";
RL Cell. Microbiol. 19:0-0(2017).
RN [8] {ECO:0007744|PDB:6EFC, ECO:0007744|PDB:6EFD}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 220-453.
RA Iverson T.M.;
RT "Engineering sialoglycan selectivity through structure-based optimization
RT of Siglec-like adhesins.";
RL Submitted (AUG-2018) to the PDB data bank.
CC -!- FUNCTION: A cell wall protein involved with PadA in host cell
CC interactions required for colonization and pathogensis (Probable)
CC (PubMed:19884334, PubMed:27616700). Mediates hemagglutination and
CC adherence to ghst glycoproteins (PubMed:11854202). Recognizes fetuin-A
CC (AHSG), a highly glycosylated human plasma protein, also involved in
CC recognition of human platelets, probably via platelet glycoprotein Ib
CC alpha (GP1BA) (PubMed:19884334). Acts in concert with PadA to promote
CC binding to glycosylated human fibronectin (FN1) and vitronectin (VTN),
CC and biofilm formation. Plays a major role in fibronectin and
CC vitronectin binding; binding is mediated by glycosylated regions.
CC Probably mediates interaction of PadA with resting platelets
CC (PubMed:27616700). {ECO:0000269|PubMed:11854202,
CC ECO:0000269|PubMed:19884334, ECO:0000269|PubMed:27616700,
CC ECO:0000305|PubMed:11854202}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000269|PubMed:15213130,
CC ECO:0000269|PubMed:19884334}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477}.
CC -!- DOMAIN: Has a short (SR1) and long (SR22) Ser-rich region separated by
CC 2 non-repeats regions (NR1 and NR2). SR2 is comprised of 113 inexact
CC repeats of SASTSASVSASE (PubMed:11854202). SR2 is thought to extend
CC about 0.2 um away from the cell surface (Probable). SR1, NR2 and SR2
CC are essential for Hsa-mediated hemagglutination and for binding to
CC sialoglycoconjugates (fetuin and NeuAc-alpha-2-3Gal-beta-1-4(Glc)-HSA);
CC removal of the N- or C-terminus of SR2 (residues 448-1459 or 1092-2143
CC respectively) still allows binding and hemagglutination
CC (PubMed:15213130). {ECO:0000269|PubMed:11854202,
CC ECO:0000269|PubMed:15213130, ECO:0000305|PubMed:11854202}.
CC -!- PTM: The protein is glycosylated in vivo; constructs without SR1 and
CC SR2 are not glycosylated. {ECO:0000269|PubMed:15213130,
CC ECO:0000269|PubMed:27616700}.
CC -!- DISRUPTION PHENOTYPE: Loss of bacterial-mediated red blood cell
CC hemagglutination, no bacterial adhesion to glycoconjugates with alpha-
CC 2-3 sialic acid termini (PubMed:11854202). No longer aggregates human
CC platelets (PubMed:15213130). Bacteria no longer bind human fetuin.
CC Bacteria bind less well to human platelets. Triple sspA-sspB-hsa
CC deletion no longer causes human platelet aggregation; a single hsa
CC deletion aggregates platelets normally. Significantly reduced binding
CC to human glycocalicin (GP1BA, the shed form of platelet glycoprotein Ib
CC alpha) (PubMed:19884334). No change in platelet spreading on S.gordonii
CC (PubMed:21071690). Single mutant no longer binds to vitronectin (VTN)
CC and fibronectin (FN1), slightly less well to salivary pellicle and
CC makes less biofilm on salivary pellicle. Double hsa-padA deletions bind
CC less well to human platelets than does the single padA deletion and
CC make no biofilm on salivary pellicle (PubMed:27616700).
CC {ECO:0000269|PubMed:11854202, ECO:0000269|PubMed:15213130,
CC ECO:0000269|PubMed:19884334, ECO:0000269|PubMed:21071690,
CC ECO:0000269|PubMed:27616700}.
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 serine-rich repeat protein (SRRP) family.
CC {ECO:0000305}.
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DR EMBL; AB029393; BAA97453.1; -; Genomic_DNA.
DR EMBL; CP000725; ABV10391.1; -; Genomic_DNA.
DR PDB; 6EFC; X-ray; 1.40 A; A=220-453.
DR PDB; 6EFD; X-ray; 1.85 A; A=220-453.
DR PDB; 6X3K; X-ray; 2.50 A; A=220-453.
DR PDB; 6X3Q; X-ray; 2.15 A; A=220-453.
DR PDBsum; 6EFC; -.
DR PDBsum; 6EFD; -.
DR PDBsum; 6X3K; -.
DR PDBsum; 6X3Q; -.
DR AlphaFoldDB; A8AWU7; -.
DR SMR; A8AWU7; -.
DR STRING; 467705.SGO_0966; -.
DR EnsemblBacteria; ABV10391; ABV10391; SGO_0966.
DR KEGG; sgo:SGO_0966; -.
DR eggNOG; COG3147; Bacteria.
DR eggNOG; COG5295; Bacteria.
DR HOGENOM; CLU_227392_0_0_9; -.
DR OMA; DTTHPPA; -.
DR Proteomes; UP000001131; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0098785; P:biofilm matrix assembly; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0090604; P:surface biofilm formation; IMP:UniProtKB.
DR InterPro; IPR044024; aRib.
DR InterPro; IPR022263; KxYKxGKxW.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR026465; Ser_adhes_glycop.
DR Pfam; PF18938; aRib; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF19258; KxYKxGKxW_sig; 1.
DR TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
DR TIGRFAMs; TIGR04224; ser_adhes_Nterm; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell wall; Glycoprotein; Peptidoglycan-anchor;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..90
FT /evidence="ECO:0000305|PubMed:15213130"
FT CHAIN 91..2178
FT /note="Streptococcal hemagglutinin"
FT /id="PRO_0000452687"
FT PROPEP 2148..2178
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_5018364652"
FT REGION 91..137
FT /note="Non-repeat region 1 (NR1)"
FT /evidence="ECO:0000269|PubMed:11854202"
FT REGION 138..219
FT /note="Ser-rich region 1 (SR1)"
FT /evidence="ECO:0000269|PubMed:11854202"
FT REGION 192..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..449
FT /note="Non-repeat region 2 (NR2)"
FT /evidence="ECO:0000269|PubMed:11854202"
FT REGION 450..2143
FT /note="Ser-rich region 2 (SR2)"
FT /evidence="ECO:0000269|PubMed:11854202"
FT REGION 495..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1725..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2119..2151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2144..2148
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 192..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2119..2150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2147
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 381..382
FT /note="DP -> ES (in Ref. 1; BAA97453)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="S -> Y (in Ref. 1; BAA97453)"
FT /evidence="ECO:0000305"
FT CONFLICT 1396
FT /note="S -> C (in Ref. 1; BAA97453)"
FT /evidence="ECO:0000305"
FT CONFLICT 1419
FT /note="I -> V (in Ref. 1; BAA97453)"
FT /evidence="ECO:0000305"
FT CONFLICT 1492..1495
FT /note="SASE -> CASA (in Ref. 1; BAA97453)"
FT /evidence="ECO:0000305"
FT CONFLICT 1507
FT /note="E -> G (in Ref. 1; BAA97453)"
FT /evidence="ECO:0000305"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6X3K"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6EFD"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 333..345
FT /evidence="ECO:0007829|PDB:6EFC"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:6EFC"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:6EFC"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:6EFC"
FT HELIX 395..408
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:6EFC"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:6EFC"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:6EFC"
SQ SEQUENCE 2178 AA; 203539 MW; F2265397E5C467AF CRC64;
MFFKRQKGQY HEVERVTRFK LIKSGKHWLR AATSQFGLLR LMKGADISSV EVKVAEEQSV
EKGGLNYLKG IIATGAVLGG AVVTSSSVYA EEEQALEKVI DTRDVLATRG EAVLSEEAAT
TLSSEGANPV ESLSDTLSAS ESASANSVST SISISESFSV SASASLSSSS SLSQSSSESA
SASESLSVSA STSQSFSSTT SSTQSSNNES LISSDSSNSL NTNQSVSARN QNARVRTRRA
VAANDTEAPQ VKSGDYVVYR GESFEYYAEI TDNSGQVNRV VIRNVEGGAN STYLSPNWVK
YSTENLGRPG NATVQNPLRT RIFGEVPLNE IVNEKSYYTR YIVAWDPSGN ATQMVDNANR
NGLERFVLTV KSQNEKYDPA DPSVTYVNNL SNLSTSEREA VAAAVRAANP NIPPTAKITV
SQNGTVTITY PDKSTDTIPA NRVVKDLQIS KSNSASQSSS VSASQSASTS VSASISASMS
ASVSVSTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASKSSSTSAS VSASESASTS
ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS
ASVSASESAS TSASVSASES ASTSASVSAS ESSSTSASVS ASESASTSAS VSASESASTS
ASVSASTSAS TSASVSASTS ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS
ASVSASTSAS TSASVSASTS ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS
ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS
ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS
ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS
ASVSASESAS TSASVSASES ASTSASISAS ESASTSASVS ASESASTSAS VSASTSASTS
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS
ASVSASTSAS TSASVSASES SSTSASVSAS ESASTSSSVS ASESASTSAS VSASESASTS
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS
ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS
ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASMS
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS
ASVSASESAS TSASVSASES AYTSASASAS ESASTSASIS ASESASTSAS VSASESAYTS
ASVSASESGS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESSSTS
ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS
ASVSASESAS TSASVSTSES ASTSASVSAS ESASTSASVS ASESASTSAS VSASESSSTS
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSVS VSASESASTS
ASVSASESAS SSASVSASKS ASMSASVLAS ESASTSASVS ASESASTSAS VSASESASTS
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS VSASTSASTS
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESVSANES ASTSASVSAS
TSASTSASVS SSESASTSAS VSASESASTS ASVSASESAS TSASVSASES ASISASISAS
ESSSTSASVS ASESASTSAS VSASTSTSTS ASVSASESAS TSASVFASES ASTSASVSAS
ESASTSASVS ASTSASTSAS VSASESASTS ASISASESAS TSASISASES SSTSASVSAS
TSASTSASVS ASESTSTSVS ISASESVSIS TSVSQSMSVS ESLSLSVSTS TLHSQLNGIY
ESELNSLSLS ESLSMSQSLS QSLSDSQSTS ATQSMHDRIS KGQLPRTGES ESKASILALG
IGALGLAFKK RKKNESED
