CHIPS_STAAE
ID CHIPS_STAAE Reviewed; 149 AA.
AC A6QIG7; Q7WUJ0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, 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=NWMN_1877;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-60, FUNCTION,
RP SUBCELLULAR LOCATION, AND PROPHAGE-ENCODED PROTEIN.
RX PubMed=14993252; DOI=10.1084/jem.20031636;
RA de Haas C.J.C., Veldkamp K.E., Peschel A., Weerkamp F., van Wamel W.J.B.,
RA Heezius E.C.J.M., Poppelier M.J.J.G., van Kessel K.P.M., van Strijp J.A.G.;
RT "Chemotaxis inhibitory protein of Staphylococcus aureus, a bacterial
RT antiinflammatory agent.";
RL J. Exp. Med. 199:687-695(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [3]
RP FUNCTION, AND INTERACTION WITH HUMAN C5AR AND FPR.
RX PubMed=15153520; DOI=10.4049/jimmunol.172.11.6994;
RA Postma B., Poppelier M.J.J.G., van Galen J.C., Prossnitz E.R.,
RA van Strijp J.A.G., de Haas C.J.C., van Kessel K.P.M.;
RT "Chemotaxis inhibitory protein of Staphylococcus aureus binds specifically
RT to the C5a and formylated peptide receptor.";
RL J. Immunol. 172:6994-7001(2004).
RN [4]
RP INTERACTION WITH HUMAN FPR, AND MUTAGENESIS OF PHE-29 AND PHE-31.
RX PubMed=15494522; DOI=10.4049/jimmunol.173.9.5704;
RA Haas P.-J., de Haas C.J.C., Kleibeuker W., Poppelier M.J.J.G.,
RA van Kessel K.P.M., Kruijtzer J.A.W., Liskamp R.M.J., van Strijp J.A.G.;
RT "N-terminal residues of the chemotaxis inhibitory protein of Staphylococcus
RT aureus are essential for blocking formylated peptide receptor but not C5a
RT receptor.";
RL J. Immunol. 173:5704-5711(2004).
RN [5]
RP INTERACTION WITH HUMAN C5AR.
RX PubMed=15542591; DOI=10.1074/jbc.m412230200;
RA Postma B., Kleibeuker W., Poppelier M.J.J.G., Boonstra M.,
RA van Kessel K.P.M., van Strijp J.A.G., de Haas C.J.C.;
RT "Residues 10-18 within the C5a receptor N terminus compose a binding domain
RT for chemotaxis inhibitory protein of Staphylococcus aureus.";
RL J. Biol. Chem. 280:2020-2027(2005).
RN [6]
RP PROPHAGE-ENCODED PROTEIN.
RX PubMed=16452413; DOI=10.1128/jb.188.4.1310-1315.2006;
RA van Wamel W.J.B., Rooijakkers S.H.M., Ruyken M., van Kessel K.P.M.,
RA van Strijp J.A.G.;
RT "The innate immune modulators staphylococcal complement inhibitor and
RT chemotaxis inhibitory protein of Staphylococcus aureus are located on beta-
RT hemolysin-converting bacteriophages.";
RL J. Bacteriol. 188:1310-1315(2006).
RN [7]
RP PROPHAGE-ENCODED PROTEIN.
RX PubMed=17078814; DOI=10.1111/j.1365-2958.2006.05441.x;
RA Bae T., Baba T., Hiramatsu K., Schneewind O.;
RT "Prophages of Staphylococcus aureus Newman and their contribution to
RT virulence.";
RL Mol. Microbiol. 62:1035-1047(2006).
RN [8]
RP STRUCTURE BY NMR OF 59-149, AND MUTAGENESIS OF LYS-68; ARG-72; ARG-74;
RP LYS-78; LYS-79; LYS-82; LYS-89; LYS-97; ARG-112; LYS-113; LYS-120; LYS-123;
RP LYS-128; LYS-129; LYS-133 AND LYS-143.
RX PubMed=16213522; DOI=10.1016/j.jmb.2005.09.014;
RA Haas P.-J., de Haas C.J.C., Poppelier M.J.J.G., van Kessel K.P.M.,
RA van Strijp J.A.G., Dijkstra K., Scheek R.M., Fan H., Kruijtzer J.A.W.,
RA Liskamp R.M.J., Kemmink J.;
RT "The structure of the C5a receptor-blocking domain of chemotaxis inhibitory
RT protein of Staphylococcus aureus is related to a group of immune evasive
RT molecules.";
RL J. Mol. Biol. 353:859-872(2005).
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. {ECO:0000269|PubMed:14993252,
CC ECO:0000269|PubMed:15153520}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14993252}.
CC -!- DOMAIN: Two distinct active sites are responsible for anti-C5aR and
CC anti-FPR activity. They might be closely spatially related and might be
CC overlapping.
CC -!- MISCELLANEOUS: Encoded within a prophage region.
CC -!- SIMILARITY: Belongs to the CHIPS/FLIPr family. {ECO:0000305}.
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DR EMBL; AF285146; AAQ14339.1; -; Genomic_DNA.
DR EMBL; AP009351; BAF68149.1; -; Genomic_DNA.
DR RefSeq; WP_000727649.1; NZ_CP023390.1.
DR PDB; 1XEE; NMR; -; A=59-149.
DR PDB; 2K3U; NMR; -; A=59-149.
DR PDBsum; 1XEE; -.
DR PDBsum; 2K3U; -.
DR AlphaFoldDB; A6QIG7; -.
DR BMRB; A6QIG7; -.
DR SMR; A6QIG7; -.
DR EnsemblBacteria; BAF68149; BAF68149; NWMN_1877.
DR KEGG; sae:NWMN_1877; -.
DR HOGENOM; CLU_1748521_0_0_9; -.
DR EvolutionaryTrace; A6QIG7; -.
DR PRO; PR:A6QIG7; -.
DR Proteomes; UP000006386; 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 3D-structure; Direct protein sequencing; Secreted; Signal; Virulence.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:14993252"
FT CHAIN 29..149
FT /note="Chemotaxis inhibitory protein"
FT /id="PRO_0000319608"
FT REGION 29..34
FT /note="FPR-blocking activity"
FT REGION 59..149
FT /note="C5aR-blocking activity"
FT MUTAGEN 29
FT /note="F->A: Abolishes FPR-blocking activity. No effect on
FT C5aR-blocking activity."
FT /evidence="ECO:0000269|PubMed:15494522"
FT MUTAGEN 29
FT /note="Missing: Abolishes FPR-blocking activity. No effect
FT on C5aR-blocking activity."
FT /evidence="ECO:0000269|PubMed:15494522"
FT MUTAGEN 31
FT /note="F->A: Decreases FPR-blocking activity. No effect on
FT C5aR-blocking activity."
FT /evidence="ECO:0000269|PubMed:15494522"
FT MUTAGEN 68
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 72
FT /note="R->A: Decreases C5aR-blocking activity. No effect on
FT FPR-blocking activity."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 74
FT /note="R->A: Decreases both C5aR- and FPR-blocking
FT activity."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 78
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 79
FT /note="K->A: Slightly decreases C5aR-blocking activity. No
FT effect on FPR-blocking activity."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 82
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 89
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 97
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 112
FT /note="R->A: Decreases both C5aR- and FPR-blocking
FT activity."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 113
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 120
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 123
FT /note="K->A: Decreases C5aR-blocking activity. No effect on
FT FPR-blocking activity."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 128
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 129
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 133
FT /note="K->A: Slightly decreases C5aR-blocking activity. No
FT effect on FPR-blocking activity."
FT /evidence="ECO:0000269|PubMed:16213522"
FT MUTAGEN 143
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:16213522"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:1XEE"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1XEE"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:1XEE"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1XEE"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:1XEE"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1XEE"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1XEE"
SQ SEQUENCE 149 AA; 17058 MW; 6F5CC73C5BDB36AC CRC64;
MKKKLATTVL ALSFLTAGIS THHHSAKAFT FEPFPTNEEI ESNKKMLEKE KAYKESFKNS
GLPTTLGKLD ERLRNYLKKG TKNSAQFEKM VILTENKGYY TVYLNTPLAE DRKNVELLGK
MYKTYFFKKG ESKSSYVING PGKTNEYAY
