SPA_STAAM
ID SPA_STAAM Reviewed; 450 AA.
AC P0A015; Q99XA2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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; OrderedLocusNames=SAV0111;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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 -!- MISCELLANEOUS: Unlike many other strains of S.aureus, SpA has only 4
CC Ig-binding domains in Mu50. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin-binding protein SpA family.
CC {ECO:0000305}.
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DR EMBL; BA000017; BAB56273.1; -; Genomic_DNA.
DR RefSeq; WP_000728765.1; NC_002758.2.
DR PDB; 4HJG; X-ray; 2.00 A; H=101-151.
DR PDB; 4HKZ; X-ray; 2.08 A; H=101-151.
DR PDB; 4IOI; X-ray; 1.95 A; H=101-151.
DR PDBsum; 4HJG; -.
DR PDBsum; 4HKZ; -.
DR PDBsum; 4IOI; -.
DR AlphaFoldDB; P0A015; -.
DR SMR; P0A015; -.
DR PaxDb; P0A015; -.
DR ABCD; P0A015; 1 sequenced antibody.
DR EnsemblBacteria; BAB56273; BAB56273; SAV0111.
DR KEGG; sav:SAV0111; -.
DR HOGENOM; CLU_024983_1_0_9; -.
DR OMA; QRNGYIQ; -.
DR BioCyc; SAUR158878:SAV_RS00690-MON; -.
DR PRO; PR:P0A015; -.
DR Proteomes; UP000002481; Chromosome.
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; 4.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF03373; Octapeptide; 10.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF46997; SSF46997; 4.
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; IgG-binding protein; Peptidoglycan-anchor; Repeat;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..419
FT /note="Immunoglobulin G-binding protein A"
FT /id="PRO_0000005649"
FT PROPEP 420..450
FT /note="Removed by sortase"
FT /evidence="ECO:0000250|UniProtKB:P02976,
FT ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005650"
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/C"
FT /evidence="ECO:0000305"
FT REPEAT 268..275
FT /note="2-1"
FT REPEAT 276..283
FT /note="2-2"
FT REPEAT 284..291
FT /note="2-3"
FT REPEAT 292..299
FT /note="2-4"
FT REPEAT 300..307
FT /note="2-5"
FT REPEAT 308..315
FT /note="2-6"
FT REPEAT 316..323
FT /note="2-7"
FT REPEAT 324..331
FT /note="2-8"
FT REPEAT 332..339
FT /note="2-9"
FT REPEAT 340..347
FT /note="2-10"
FT REPEAT 348..355
FT /note="2-11"
FT DOMAIN 355..399
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 260..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..355
FT /note="12 X 8 AA approximate tandem repeats"
FT REGION 401..421
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 416..420
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 260..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 419
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:4IOI"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:4IOI"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4IOI"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:4IOI"
SQ SEQUENCE 450 AA; 48873 MW; 7BBA8C8578FB1549 CRC64;
MKKKNIYSIR KLGVGIASVT LGTLLISGGV TPAANAAQHD EAQQNAFYQV LNMPNLNADQ
RNGFIQSLKD DPSQSANVLG EAQKLNDSQA PKADAQQNNF NKDQQSAFYE ILNMPNLNEA
QRNGFIQSLK DDPSQSTNVL GEAKKLNESQ APKADNNFNK EQQNAFYEIL NMPNLNEEQR
NGFIQSLKDD PSQSANLLSE AKKLNESQAP KADNKFNKEQ QNAFYEILHL PNLNEEQRNG
FIQSLKDDPS VSKEILAEAK KLNDAQAPKE EDNKKPGKED GNKPGKEDGN KPGKEDNKKP
GKEDGNKPGK EDNNKPGKED GNKPGKEDNN KPGKEDGNKP GKEDGNKPGK EDGNGVHVVK
PGDTVNDIAK ANGTTADKIA ADNKLADKNM IKPGQELVVD KKQPANHADA NKAQALPETG
EENPFIGTTV FGGLSLALGA ALLAGRRREL
