ID   CHIPS_STAAN             Reviewed;         149 AA.
AC   Q99SU8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Chemotaxis inhibitory protein;
DE   AltName: Full=CHIPS;
DE   Flags: Precursor;
GN   Name=chp; OrderedLocusNames=SA1755;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
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: 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; BA000018; BAB43029.1; -; Genomic_DNA.
DR   PIR; E89983; E89983.
DR   RefSeq; WP_000727645.1; NC_002745.2.
DR   AlphaFoldDB; Q99SU8; -.
DR   BMRB; Q99SU8; -.
DR   SMR; Q99SU8; -.
DR   EnsemblBacteria; BAB43029; BAB43029; BAB43029.
DR   KEGG; sau:SA1755; -.
DR   HOGENOM; CLU_1748521_0_0_9; -.
DR   PRO; PR:Q99SU8; -.
DR   Proteomes; UP000000751; 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_0000319606"
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;  17073 MW;  54EEDE97E9CF26A4 CRC64;
     MKKKLATTVL ALSFLTAGIS THHHSAKAFT FEPFPTNEEI ESNKKMLEKE KAYKESFKNS
     GLPTTLGKLD ERLRNYLEKG TKNTAQFEKM VILTENKGYY TVYLNTPLAE DRKNVELLGK
     MYKTYFFKKG ESKSSYVING PGKTNEYAY