ID   CHIPS_STAAR             Reviewed;         149 AA.
AC   Q6GFB3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Chemotaxis inhibitory protein;
DE   AltName: Full=CHIPS;
DE   Flags: Precursor;
GN   Name=chp; OrderedLocusNames=SAR2036;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Involved in countering the first line of host defense
CC       mechanisms. Specifically inhibits the response of human neutrophils and
CC       monocytes to complement anaphylatoxin C5a and formylated peptides, like
CC       N-formyl-methionyl-leucyl-phenylalanine (fMLP). Acts by binding
CC       directly to the C5a receptor (C5aR) and formylated peptide receptor
CC       (FPR), thereby blocking the C5a- and fMLP-induced calcium responses.
CC       Prevents phagocytosis of the bacterium (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CHIPS/FLIPr family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG41022.1; -; Genomic_DNA.
DR   RefSeq; WP_000727649.1; NC_002952.2.
DR   AlphaFoldDB; Q6GFB3; -.
DR   BMRB; Q6GFB3; -.
DR   SMR; Q6GFB3; -.
DR   KEGG; sar:SAR2036; -.
DR   HOGENOM; CLU_1748521_0_0_9; -.
DR   OrthoDB; 2115230at2; -.
DR   PRO; PR:Q6GFB3; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.10.20.390; -; 1.
DR   InterPro; IPR020986; CHIPS.
DR   InterPro; IPR038529; FLIPR/CHIP_sf.
DR   InterPro; IPR023253; FLIPR/CHIPS.
DR   Pfam; PF11434; CHIPS; 1.
DR   PRINTS; PR02036; CHEMOTAXISIP.
DR   PRINTS; PR02035; FLIPRCHIPS.
PE   3: Inferred from homology;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   CHAIN           29..149
FT                   /note="Chemotaxis inhibitory protein"
FT                   /id="PRO_0000319605"
FT   REGION          29..34
FT                   /note="FPR-blocking activity"
FT                   /evidence="ECO:0000250"
FT   REGION          59..149
FT                   /note="C5aR-blocking activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   149 AA;  17058 MW;  6F5CC73C5BDB36AC CRC64;
     MKKKLATTVL ALSFLTAGIS THHHSAKAFT FEPFPTNEEI ESNKKMLEKE KAYKESFKNS
     GLPTTLGKLD ERLRNYLKKG TKNSAQFEKM VILTENKGYY TVYLNTPLAE DRKNVELLGK
     MYKTYFFKKG ESKSSYVING PGKTNEYAY