ID   CHIPS_STAA8             Reviewed;         149 AA.
AC   Q2FWV5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Chemotaxis inhibitory protein;
DE   AltName: Full=CHIPS;
DE   Flags: Precursor;
GN   Name=chp; OrderedLocusNames=SAOUHSC_02169;
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   CHARACTERIZATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=16882032; DOI=10.1111/j.1462-5822.2006.00709.x;
RA   Rooijakkers S.H.M., Ruyken M., van Roon J., van Kessel K.P.M.,
RA   van Strijp J.A.G., van Wamel W.J.B.;
RT   "Early expression of SCIN and CHIPS drives instant immune evasion by
RT   Staphylococcus aureus.";
RL   Cell. Microbiol. 8:1282-1293(2006).
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 (By
CC       similarity). Prevents phagocytosis of the bacterium. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed maximally during the exponential growth
CC       phase. {ECO:0000269|PubMed:16882032}.
CC   -!- INDUCTION: Up-regulated by sae locus. Down-regulated by SarA and sigma
CC       B factor. {ECO:0000269|PubMed:16882032}.
CC   -!- SIMILARITY: Belongs to the CHIPS/FLIPr family. {ECO:0000305}.
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DR   EMBL; CP000253; ABD31214.1; -; Genomic_DNA.
DR   RefSeq; WP_000727643.1; NZ_LS483365.1.
DR   RefSeq; YP_500656.1; NC_007795.1.
DR   AlphaFoldDB; Q2FWV5; -.
DR   BMRB; Q2FWV5; -.
DR   SMR; Q2FWV5; -.
DR   EnsemblBacteria; ABD31214; ABD31214; SAOUHSC_02169.
DR   GeneID; 3921863; -.
DR   KEGG; sao:SAOUHSC_02169; -.
DR   PATRIC; fig|93061.5.peg.1967; -.
DR   HOGENOM; CLU_1748521_0_0_9; -.
DR   PRO; PR:Q2FWV5; -.
DR   Proteomes; UP000008816; 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   1: Evidence at protein level;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   CHAIN           29..149
FT                   /note="Chemotaxis inhibitory protein"
FT                   /id="PRO_0000319607"
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;  17040 MW;  8F4896794F8B23AD CRC64;
     MKKKLATTVL ALSFLTAGIS THHHSAKAFT FEPFPTNEEI ESNKKLLEKE KAYKESFKNS
     GLPTTLGKLD ERLRNYLKKG TKNSAQFEKM VILTENKGYY TVYLNTPLAE DRKNVELLGK
     MYKTYFFKKG ESKSSYVING PGKTNEYAY