SASG_STAA8
ID SASG_STAA8 Reviewed; 1627 AA.
AC Q2G2B2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Surface protein G;
DE Flags: Precursor;
GN Name=sasG; OrderedLocusNames=SAOUHSC_02798;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE A.
RC STRAIN=RN4220;
RX PubMed=11830639; DOI=10.1073/pnas.032523999;
RA Mazmanian S.K., Ton-That H., Su K., Schneewind O.;
RT "An iron-regulated sortase anchors a class of surface protein during
RT Staphylococcus aureus pathogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2293-2298(2002).
RN [3]
RP INVOLVEMENT IN HUMAN INFECTION.
RX PubMed=12634333; DOI=10.1099/mic.0.25996-0;
RA Roche F.M., Massey R., Peacock S.J., Day N.P.J., Visai L., Speziale P.,
RA Lam A., Pallen M., Foster T.J.;
RT "Characterization of novel LPXTG-containing proteins of Staphylococcus
RT aureus identified from genome sequences.";
RL Microbiology 149:643-654(2003).
RN [4]
RP FUNCTION IN NASAL COLONIZATION.
RX PubMed=14523109; DOI=10.1099/mic.0.26412-0;
RA Roche F.M., Meehan M., Foster T.J.;
RT "The Staphylococcus aureus surface protein sasG and its homologues promote
RT bacterial adherence to human desquamated nasal epithelial cells.";
RL Microbiology 149:2759-2767(2003).
RN [5]
RP FUNCTION IN BIOFILM FORMATION, AND MORPHOLOGY.
RX PubMed=17660408; DOI=10.1099/mic.0.2007/006676-0;
RA Corrigan R.M., Rigby D., Handley P., Foster T.J.;
RT "The role of Staphylococcus aureus surface protein sasG in adherence and
RT biofilm formation.";
RL Microbiology 153:2435-2446(2007).
CC -!- FUNCTION: Promotes adhesion of bacterial cells to human squamous nasal
CC epithelial cells, a phenomenon which is likely to be important in nasal
CC colonization. Forms short, extremely dense and thin fibrils all over
CC the bacterial surface. Does not bind to either buccal cells or non-
CC differentiated keratinocytes. Promotes cellular aggregation leading to
CC biofilm formation. {ECO:0000269|PubMed:14523109,
CC ECO:0000269|PubMed:17660408}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000305|PubMed:11830639}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639}.
CC Note=Anchored to the cell wall by sortase A.
CC {ECO:0000305|PubMed:11830639}.
CC -!- MISCELLANEOUS: Produced during infection of the human host. Does not
CC bind to immobilized fibrinogen, fibronectin, IgG, human epidermal
CC keratin, collagen, vWF, laminin, heparan sulfate and submaxillary
CC mucin.
CC -!- MISCELLANEOUS: When sasG is expressed at high levels, it inhibits
CC adhesion of S.aureus to the ligands fibrinogen, fibronectin,
CC cytokeratin 10 and IgG. This inhibitory effect depends on the number of
CC G5 repeats present in the protein, since shorter variants do not
CC present this phenotype.
CC -!- MISCELLANEOUS: Biofilm formation is ica-independent, relying only on
CC the level of expression of the protein and the number of G5 repeats.
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DR EMBL; CP000253; ABD31801.1; -; Genomic_DNA.
DR RefSeq; WP_001205091.1; NC_007795.1.
DR RefSeq; YP_501257.1; NC_007795.1.
DR PDB; 3TIP; X-ray; 1.70 A; A=502-629.
DR PDB; 3TIQ; X-ray; 1.87 A; A/B=419-629.
DR PDB; 4WVE; X-ray; 1.60 A; A/B=545-757.
DR PDB; 5DBL; X-ray; 1.60 A; A=502-629.
DR PDBsum; 3TIP; -.
DR PDBsum; 3TIQ; -.
DR PDBsum; 4WVE; -.
DR PDBsum; 5DBL; -.
DR AlphaFoldDB; Q2G2B2; -.
DR SASBDB; Q2G2B2; -.
DR SMR; Q2G2B2; -.
DR STRING; 1280.SAXN108_2744; -.
DR PRIDE; Q2G2B2; -.
DR EnsemblBacteria; ABD31801; ABD31801; SAOUHSC_02798.
DR GeneID; 3921452; -.
DR KEGG; sao:SAOUHSC_02798; -.
DR PATRIC; fig|93061.5.peg.2530; -.
DR eggNOG; COG3583; Bacteria.
DR HOGENOM; CLU_000977_4_0_9; -.
DR OMA; IWEANIS; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0090609; P:single-species submerged biofilm formation; IDA:CACAO.
DR InterPro; IPR011098; G5_dom.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR031477; SasG_E.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF07501; G5; 9.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF17041; SasG_E; 8.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM01208; G5; 9.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS51109; G5; 9.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Peptidoglycan-anchor; Reference proteome; Repeat;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..1598
FT /note="Surface protein G"
FT /id="PRO_0000323595"
FT PROPEP 1599..1627
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:11830639"
FT /id="PRO_0000323596"
FT DOMAIN 419..501
FT /note="G5 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT DOMAIN 547..629
FT /note="G5 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT DOMAIN 675..757
FT /note="G5 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT DOMAIN 803..885
FT /note="G5 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT DOMAIN 931..1013
FT /note="G5 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT DOMAIN 1059..1141
FT /note="G5 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT DOMAIN 1187..1269
FT /note="G5 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT DOMAIN 1315..1397
FT /note="G5 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT DOMAIN 1443..1525
FT /note="G5 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT REGION 51..418
FT /note="Ligand binding A region, squamous nasal epithelial
FT cell binding"
FT REGION 74..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 22..33
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000305"
FT MOTIF 1595..1599
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 92..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1598
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT STRAND 423..433
FT /evidence="ECO:0007829|PDB:3TIQ"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:3TIQ"
FT STRAND 450..454
FT /evidence="ECO:0007829|PDB:3TIQ"
FT STRAND 459..469
FT /evidence="ECO:0007829|PDB:3TIQ"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:3TIQ"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:3TIQ"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:3TIQ"
FT STRAND 493..497
FT /evidence="ECO:0007829|PDB:3TIQ"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:3TIQ"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:5DBL"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:5DBL"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:5DBL"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:5DBL"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:5DBL"
FT STRAND 543..547
FT /evidence="ECO:0007829|PDB:5DBL"
FT STRAND 555..561
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 587..593
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:4WVE"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 604..607
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 611..616
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 634..638
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 647..650
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:4WVE"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 671..675
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 683..689
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 693..697
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 706..710
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 715..721
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:4WVE"
FT TURN 727..729
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 732..735
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 739..744
FT /evidence="ECO:0007829|PDB:4WVE"
FT STRAND 749..753
FT /evidence="ECO:0007829|PDB:4WVE"
SQ SEQUENCE 1627 AA; 178527 MW; EBCC84B4167A729D CRC64;
MRDKKGPVNK RVDFLSNKLN KYSIRKFTVG TASILIGSLM YLGTQQEAEA AENNIENPTT
LKDNVQSKEV KIEEVTNKDT APQGVEAKSE VTSNKDTIEH EPSVKAEDIS KKEDTPKEVA
DVAEVQPKSS VTHNAETPKV RKARSVDEGS FDITRDSKNV VESTPITIQG KEHFEGYGSV
DIQKKPTDLG VSEVTRFNVG NESNGLIGAL QLKNKIDFSK DFNFKVRVAN NHQSNTTGAD
GWGFLFSKGN AEEYLTNGGI LGDKGLVNSG GFKIDTGYIY TSSMDKTEKQ AGQGYRGYGA
FVKNDSSGNS QMVGENIDKS KTNFLNYADN STNTSDGKFH GQRLNDVILT YVASTGKMRA
EYAGKTWETS ITDLGLSKNQ AYNFLITSSQ RWGLNQGINA NGWMRTDLKG SEFTFTPEAP
KTITELEKKV EEIPFKKERK FNPDLAPGTE KVTREGQKGE KTITTPTLKN PLTGVIISKG
EPKEEITKDP INELTEYGPE TIAPGHRDEF DPKLPTGEKE EVPGKPGIKN PETGDVVRPP
VDSVTKYGPV KGDSIVEKEE IPFEKERKFN PDLAPGTEKV TREGQKGEKT ITTPTLKNPL
TGEIISKGES KEEITKDPIN ELTEYGPETI TPGHRDEFDP KLPTGEKEEV PGKPGIKNPE
TGDVVRPPVD SVTKYGPVKG DSIVEKEEIP FEKERKFNPD LAPGTEKVTR EGQKGEKTIT
TPTLKNPLTG VIISKGEPKE EITKDPINEL TEYGPETITP GHRDEFDPKL PTGEKEEVPG
KPGIKNPETG DVVRPPVDSV TKYGPVKGDS IVEKEEIPFK KERKFNPDLA PGTEKVTREG
QKGEKTITTP TLKNPLTGEI ISKGESKEEI TKDPINELTE YGPETITPGH RDEFDPKLPT
GEKEEVPGKP GIKNPETGDV VRPPVDSVTK YGPVKGDSIV EKEEIPFEKE RKFNPDLAPG
TEKVTREGQK GEKTITTPTL KNPLTGEIIS KGESKEEITK DPINELTEYG PETITPGHRD
EFDPKLPTGE KEEVPGKPGI KNPETGDVVR PPVDSVTKYG PVKGDSIVEK EEIPFKKERK
FNPDLAPGTE KVTREGQKGE KTITTPTLKN PLTGEIISKG ESKEEITKDP INELTEYGPE
TITPGHRDEF DPKLPTGEKE EVPGKPGIKN PETGDVVRPP VDSVTKYGPV KGDSIVEKEE
IPFEKERKFN PDLAPGTEKV TREGQKGEKT ITTPTLKNPL TGEIISKGES KEEITKDPIN
ELTEYGPETI TPGHRDEFDP KLPTGEKEEV PGKPGIKNPE TGDVVRPPVD SVTKYGPVKG
DSIVEKEEIP FEKERKFNPD LAPGTEKVTR EGQKGEKTIT TPTLKNPLTG EIISKGESKE
EITKDPVNEL TEFGGEKIPQ GHKDIFDPNL PTDQTEKVPG KPGIKNPDTG KVIEEPVDDV
IKHGPKTGTP ETKTVEIPFE TKREFNPKLQ PGEERVKQEG QPGSKTITTP ITVNPLTGEK
VGEGQPTEEI TKQPVDKIVE FGGEKPKDPK GPENPEKPSR PTHPSGPVNP NNPGLSKDRA
KPNGPVHSMD KNDKVKKSKI AKESVANQEK KRAELPKTGL ESTQKGLIFS SIIGIAGLML
LARRRKN
