SPA_STAAU
ID SPA_STAAU Reviewed; 508 AA.
AC P38507;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Immunoglobulin G-binding protein A;
DE Short=IgG-binding protein A;
DE AltName: Full=Staphylococcal protein A;
DE Short=SpA;
DE Flags: Precursor;
GN Name=spa;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12598 / Cowan 1 / DSM 20372 / NCIMB 11787 / NCTC 8530;
RX PubMed=2828190; DOI=10.1016/0378-1119(87)90383-0;
RA Shuttleworth H.L., Duggleby C.J., Jones S.A., Atkinson T., Minton N.P.;
RT "Nucleotide sequence analysis of the gene for protein A from Staphylococcus
RT aureus Cowan 1 (NCTC8530) and its enhanced expression in Escherichia
RT coli.";
RL Gene 58:283-295(1987).
RN [2]
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 12598 / Cowan 1 / DSM 20372 / NCIMB 11787 / NCTC 8530;
RX PubMed=913410; DOI=10.1111/j.1432-1033.1977.tb11760.x;
RA Sjoedahl J.;
RT "Structural studies on the four repetitive Fc-binding regions in protein A
RT from Staphylococcus aureus.";
RL Eur. J. Biochem. 78:471-490(1977).
RN [3] {ECO:0007744|PDB:1BDC, ECO:0007744|PDB:1BDD}
RP STRUCTURE BY NMR OF 212-270.
RX PubMed=1390743; DOI=10.1021/bi00155a020;
RA Gouda H., Torigoe H., Saito A., Sato M., Arata Y., Shimada I.;
RT "Three-dimensional solution structure of the B domain of staphylococcal
RT protein A: comparisons of the solution and crystal structures.";
RL Biochemistry 31:9665-9672(1992).
RN [4] {ECO:0007744|PDB:1EDI, ECO:0007744|PDB:1EDJ, ECO:0007744|PDB:1EDK, ECO:0007744|PDB:1EDL}
RP STRUCTURE BY NMR OF 37-92.
RX PubMed=8952510; DOI=10.1021/bi961409x;
RA Starovasnik M.A., Skelton N.J., O'Connell M.P., Kelley R.F., Reilly D.,
RA Fairbrother W.J.;
RT "Solution structure of the E-domain of staphylococcal protein A.";
RL Biochemistry 35:15558-15569(1996).
RN [5] {ECO:0007744|PDB:2SPZ}
RP STRUCTURE BY NMR OF 212-269.
RX PubMed=9325113; DOI=10.1006/jmbi.1997.1265;
RA Tashiro M., Tejero R., Zimmerman D.E., Celda B., Nilsson B.,
RA Montelione G.T.;
RT "High-resolution solution NMR structure of the Z domain of staphylococcal
RT protein A.";
RL J. Mol. Biol. 272:573-590(1997).
CC -!- FUNCTION: Plays a role in the inhibition of the host innate and
CC adaptive immune responses. Possesses five immunoglobulin-binding
CC domains that capture both the fragment crystallizable region (Fc
CC region) and the Fab region (part of Ig that identifies antigen) of
CC immunoglobulins (By similarity). In turn, Staphylococcus aureus is
CC protected from phagocytic killing via inhibition of Ig Fc region. In
CC addition, the host elicited B-cell response is prevented due to a
CC decrease of antibody-secreting cell proliferation that enter the bone
CC marrow, thereby decreasing long-term antibody production. Inhibits
CC osteogenesis by preventing osteoblast proliferation and expression of
CC alkaline phosphatase, type I collagen, osteopontin and osteocalcin.
CC Acts directly as a pro-inflammatory factor in the lung through its
CC ability to bind and activate tumor necrosis factor alpha receptor
CC 1/TNFRSF1A (By similarity). {ECO:0000250|UniProtKB:A0A0H3K686,
CC ECO:0000250|UniProtKB:P02976}.
CC -!- SUBUNIT: Interacts with host TNFRSF1A; this interaction leads to the
CC stimulation of both surface expression and shedding of TNFRSF1A.
CC {ECO:0000250|UniProtKB:A0A0H3K686}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}. Note=Anchored to the cell wall by sortase A.
CC {ECO:0000250|UniProtKB:P02976}.
CC -!- DOMAIN: Each of the immunoglobulin-binding region repeats can bind the
CC Fc region of an immunoglobulin. {ECO:0000250|UniProtKB:P02976}.
CC -!- BIOTECHNOLOGY: Important immunodiagnostic reagent because of its
CC ability to bind the Fab and Fc fragments of a wide range of mammalian
CC immunoglobulins. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin-binding protein SpA family.
CC {ECO:0000305}.
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DR EMBL; M18264; AAA26677.1; -; Genomic_DNA.
DR PIR; A29605; A29605.
DR RefSeq; WP_047211818.1; NZ_UHAY01000002.1.
DR PDB; 1BDC; NMR; -; A=212-270.
DR PDB; 1BDD; NMR; -; A=212-270.
DR PDB; 1EDI; NMR; -; A=37-92.
DR PDB; 1EDJ; NMR; -; A=37-92.
DR PDB; 1EDK; NMR; -; A=37-92.
DR PDB; 1EDL; NMR; -; A=37-92.
DR PDB; 1FC2; X-ray; 2.80 A; C=212-269.
DR PDB; 1H0T; NMR; -; A=213-269.
DR PDB; 1LP1; X-ray; 2.30 A; B=212-269.
DR PDB; 1Q2N; NMR; -; A=212-269.
DR PDB; 1SS1; NMR; -; A=212-270.
DR PDB; 2JWD; NMR; -; A=213-269.
DR PDB; 2M5A; NMR; -; A=213-269.
DR PDB; 2SPZ; NMR; -; A=212-269.
DR PDB; 3MZW; X-ray; 2.90 A; B=212-269.
DR PDB; 4NPD; X-ray; 0.90 A; A=270-327.
DR PDB; 4NPE; X-ray; 1.42 A; A=270-327.
DR PDB; 4NPF; X-ray; 1.49 A; X/Y=154-269.
DR PDB; 4WWI; X-ray; 2.31 A; A/B/C=270-327.
DR PDB; 4Y4Y; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=158-211, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=219-459.
DR PDB; 4Y5Z; X-ray; 2.95 A; 0/1/2/3/4/5/6/7/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=158-211, 0/1/2/3/4/5/6/7/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=219-459.
DR PDB; 4ZMD; X-ray; 1.87 A; A/B=270-327.
DR PDB; 4ZNC; X-ray; 2.28 A; A/B/C=270-327.
DR PDB; 5CBN; X-ray; 2.30 A; A=217-269.
DR PDB; 5CBO; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=101-153.
DR PDB; 5COC; X-ray; 2.67 A; A=213-267.
DR PDB; 5EWX; X-ray; 2.60 A; A/B=212-266.
DR PDB; 5H76; X-ray; 2.60 A; A/B/C=220-267.
DR PDB; 5H79; X-ray; 2.70 A; C/D=40-210.
DR PDB; 5H7A; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=157-209.
DR PDB; 5H7B; X-ray; 3.10 A; A/B=157-209.
DR PDB; 5H7C; X-ray; 2.70 A; A/C=99-324.
DR PDB; 5H7D; X-ray; 2.57 A; A/B/C/D/I/J/M/N=220-267.
DR PDB; 5X3F; X-ray; 3.38 A; A=220-269.
DR PDB; 5XBY; X-ray; 3.25 A; A/B/C/D=217-269.
DR PDB; 6KRV; X-ray; 3.30 A; D=212-269.
DR PDB; 7EOY; EM; 3.60 A; A/B/C=154-269.
DR PDB; 7EP6; EM; 3.86 A; A/B/C/D=154-269.
DR PDB; 7FDJ; EM; 4.40 A; A/B/C/D=154-269.
DR PDB; 7NHA; EM; 2.91 A; C=158-271.
DR PDB; 7NHC; EM; 2.87 A; C=158-271.
DR PDB; 7NHX; EM; 3.23 A; C=158-271.
DR PDB; 7NI0; EM; 3.32 A; C=158-271.
DR PDB; 7NIK; EM; 6.20 A; C=158-271.
DR PDB; 7NIL; EM; 5.01 A; C=158-271.
DR PDB; 7NIR; EM; 6.70 A; C=158-271.
DR PDB; 7NIS; EM; 5.96 A; C=158-271.
DR PDB; 7NJ3; EM; 4.48 A; C=158-271.
DR PDB; 7NJ4; EM; 5.84 A; C=158-271.
DR PDB; 7NJ5; EM; 4.63 A; C=158-271.
DR PDB; 7NJ7; EM; 4.82 A; C=158-271.
DR PDB; 7NK1; EM; 4.22 A; C=158-271.
DR PDB; 7NK2; EM; 4.84 A; C=158-271.
DR PDBsum; 1BDC; -.
DR PDBsum; 1BDD; -.
DR PDBsum; 1EDI; -.
DR PDBsum; 1EDJ; -.
DR PDBsum; 1EDK; -.
DR PDBsum; 1EDL; -.
DR PDBsum; 1FC2; -.
DR PDBsum; 1H0T; -.
DR PDBsum; 1LP1; -.
DR PDBsum; 1Q2N; -.
DR PDBsum; 1SS1; -.
DR PDBsum; 2JWD; -.
DR PDBsum; 2M5A; -.
DR PDBsum; 2SPZ; -.
DR PDBsum; 3MZW; -.
DR PDBsum; 4NPD; -.
DR PDBsum; 4NPE; -.
DR PDBsum; 4NPF; -.
DR PDBsum; 4WWI; -.
DR PDBsum; 4Y4Y; -.
DR PDBsum; 4Y5Z; -.
DR PDBsum; 4ZMD; -.
DR PDBsum; 4ZNC; -.
DR PDBsum; 5CBN; -.
DR PDBsum; 5CBO; -.
DR PDBsum; 5COC; -.
DR PDBsum; 5EWX; -.
DR PDBsum; 5H76; -.
DR PDBsum; 5H79; -.
DR PDBsum; 5H7A; -.
DR PDBsum; 5H7B; -.
DR PDBsum; 5H7C; -.
DR PDBsum; 5H7D; -.
DR PDBsum; 5X3F; -.
DR PDBsum; 5XBY; -.
DR PDBsum; 6KRV; -.
DR PDBsum; 7EOY; -.
DR PDBsum; 7EP6; -.
DR PDBsum; 7FDJ; -.
DR PDBsum; 7NHA; -.
DR PDBsum; 7NHC; -.
DR PDBsum; 7NHX; -.
DR PDBsum; 7NI0; -.
DR PDBsum; 7NIK; -.
DR PDBsum; 7NIL; -.
DR PDBsum; 7NIR; -.
DR PDBsum; 7NIS; -.
DR PDBsum; 7NJ3; -.
DR PDBsum; 7NJ4; -.
DR PDBsum; 7NJ5; -.
DR PDBsum; 7NJ7; -.
DR PDBsum; 7NK1; -.
DR PDBsum; 7NK2; -.
DR AlphaFoldDB; P38507; -.
DR SMR; P38507; -.
DR IntAct; P38507; 1.
DR MINT; P38507; -.
DR PRIDE; P38507; -.
DR ABCD; P38507; 2 sequenced antibodies.
DR PATRIC; fig|1280.4807.peg.2341; -.
DR EvolutionaryTrace; P38507; -.
DR PRO; PR:P38507; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR009063; Ig/albumin-bd_sf.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR005038; Octapeptide.
DR InterPro; IPR003132; Protein_A_Ig-bd.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF02216; B; 5.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF03373; Octapeptide; 11.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF46997; SSF46997; 5.
DR SUPFAM; SSF54106; SSF54106; 1.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Direct protein sequencing; IgG-binding protein;
KW Peptidoglycan-anchor; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..477
FT /note="Immunoglobulin G-binding protein A"
FT /id="PRO_0000005655"
FT PROPEP 478..508
FT /note="Removed by sortase"
FT /evidence="ECO:0000250|UniProtKB:P02976,
FT ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005656"
FT REPEAT 37..92
FT /note="Immunoglobulin-binding region E"
FT /evidence="ECO:0000250|UniProtKB:P02976"
FT REPEAT 93..153
FT /note="Immunoglobulin-binding region D"
FT /evidence="ECO:0000250|UniProtKB:P02976"
FT REPEAT 154..211
FT /note="Immunoglobulin-binding region A"
FT /evidence="ECO:0000250|UniProtKB:P02976"
FT REPEAT 212..269
FT /note="Immunoglobulin-binding region B"
FT /evidence="ECO:0000250|UniProtKB:P02976"
FT REPEAT 270..327
FT /note="Immunoglobulin-binding region C"
FT /evidence="ECO:0000250|UniProtKB:P02976"
FT REPEAT 333..340
FT /note="2-1"
FT REPEAT 341..348
FT /note="2-2"
FT REPEAT 349..356
FT /note="2-3"
FT REPEAT 357..364
FT /note="2-4"
FT REPEAT 365..372
FT /note="2-5"
FT REPEAT 373..380
FT /note="2-6"
FT REPEAT 381..388
FT /note="2-7"
FT REPEAT 389..396
FT /note="2-8"
FT REPEAT 397..405
FT /note="2-9"
FT REPEAT 406..413
FT /note="2-10"
FT DOMAIN 413..457
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REPEAT 414..421
FT /note="2-11"
FT REPEAT 422..429
FT /note="2-12"
FT REGION 318..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..408
FT /note="12 X 8 AA approximate tandem repeats"
FT REGION 459..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..18
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000250|UniProtKB:P02976"
FT MOTIF 474..478
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 318..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 477
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 273
FT /note="K -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:5H7C"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1EDJ"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:5H7C"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:5H7C"
FT HELIX 75..100
FT /evidence="ECO:0007829|PDB:5H7C"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:5H7A"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:5H7A"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5H7A"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:5H7A"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:4NPF"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:4NPF"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4NPF"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:4NPF"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:4NPF"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1FC2"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:4NPF"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:4NPF"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:4NPF"
FT HELIX 276..287
FT /evidence="ECO:0007829|PDB:4NPD"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:4ZMD"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:4NPD"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:4NPD"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:4NPD"
SQ SEQUENCE 508 AA; 55439 MW; E78C538D4B5E88F5 CRC64;
MKKKNIYSIR KLGVGIASVT LGTLLISGGV TPAANAAQHD EAQQNAFYQV LNMPNLNADQ
RNGFIQSLKD DPSQSANVLG EAQKLNDSQA PKADAQQNKF NKDQQSAFYE ILNMPNLNEE
QRNGFIQSLK DDPSQSTNVL GEAKKLNESQ APKADNNFNK EQQNAFYEIL NMPNLNEEQR
NGFIQSLKDD PSQSANLLAE AKKLNESQAP KADNKFNKEQ QNAFYEILHL PNLNEEQRNG
FIQSLKDDPS QSANLLAEAK KLNDAQAPKA DNKFNKEQQN AFYEILHLPN LTEEQRNGFI
QSLKDDPSVS KEILAEAKKL NDAQAPKEED NNKPGKEDGN KPGKEDGNKP GKEDNKKPGK
EDGNKPGKED NKKPGKEDGN KPGKEDGNKP GKEDGNKPGK EDGNKPGKED GNGVHVVKPG
DTVNDIAKAN GTTADKIAAD NKLADKNMIK PGQELVVDKK QPANHADANK AQALPETGEE
NPFIGTTVFG GLSLALGAAL LAGRRREL
