CNA_STAAU
ID CNA_STAAU Reviewed; 1183 AA.
AC Q53654;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Collagen adhesin;
DE Flags: Precursor;
GN Name=cna;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FDA 574;
RX PubMed=1311320; DOI=10.1016/s0021-9258(18)42898-0;
RA Patti J.M., Jonsson H., Guss B., Switalski L.M., Wiberg K., Lindberg M.,
RA Hoeoek M.;
RT "Molecular characterization and expression of a gene encoding a
RT Staphylococcus aureus collagen adhesin.";
RL J. Biol. Chem. 267:4766-4772(1992).
RN [2]
RP ERRATUM OF PUBMED:1311320.
RA Patti J.M., Jonsson H., Guss B., Switalski L.M., Wiberg K., Lindberg M.,
RA Hoeoek M.;
RL J. Biol. Chem. 269:11672-11672(1994).
RN [3]
RP DOMAIN COLLAGEN-BINDING, AND FUNCTION.
RC STRAIN=FDA 574;
RX PubMed=8218209; DOI=10.1021/bi00093a021;
RA Patti J.M., Boles J.O., Hoeoek M.;
RT "Identification and biochemical characterization of the ligand binding
RT domain of the collagen adhesin from Staphylococcus aureus.";
RL Biochemistry 32:11428-11435(1993).
RN [4]
RP FUNCTION.
RX PubMed=10816547; DOI=10.1128/iai.68.6.3776-3779.2000;
RA Rhem M.N., Lech E.M., Patti J.M., McDevitt D., Hoeoek M., Jones D.B.,
RA Wilhelmus K.R.;
RT "The collagen-binding adhesin is a virulence factor in Staphylococcus
RT aureus keratitis.";
RL Infect. Immun. 68:3776-3779(2000).
RN [5]
RP FUNCTION.
RX PubMed=15181582; DOI=10.1086/420851;
RA Xu Y., Rivas J.M., Brown E.L., Liang X., Hoeoek M.;
RT "Virulence potential of the staphylococcal adhesin CNA in experimental
RT arthritis is determined by its affinity for collagen.";
RL J. Infect. Dis. 189:2323-2333(2004).
RN [6]
RP CROSS-LINKS.
RX PubMed=18063798; DOI=10.1126/science.1145806;
RA Kang H.J., Coulibaly F., Clow F., Proft T., Baker E.N.;
RT "Stabilizing isopeptide bonds revealed in Gram-positive bacterial pilus
RT structure.";
RL Science 318:1625-1628(2007).
RN [7]
RP FUNCTION, INTERACTION WITH HOST C1QA, AND MUTAGENESIS OF TYR-175.
RC STRAIN=Phillips;
RX PubMed=23720782; DOI=10.1074/jbc.m113.454462;
RA Kang M., Ko Y.P., Liang X., Ross C.L., Liu Q., Murray B.E., Hoeoek M.;
RT "Collagen-binding microbial surface components recognizing adhesive matrix
RT molecule (MSCRAMM) of Gram-positive bacteria inhibit complement activation
RT via the classical pathway.";
RL J. Biol. Chem. 288:20520-20531(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 169-318.
RX PubMed=9334749; DOI=10.1038/nsb1097-833;
RA Symersky J., Patti J.M., Carson M., House-Pompeo K., Teale M., Moore D.,
RA Jin L., Schneider A., DeLucas L.J., Hoeoek M., Narayana S.V.L.;
RT "Structure of the collagen-binding domain from a Staphylococcus aureus
RT adhesin.";
RL Nat. Struct. Biol. 4:833-838(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 533-905, AND REGION.
RX PubMed=10673425; DOI=10.1016/s0969-2126(00)00081-2;
RA Deivanayagam C.C., Rich R.L., Carson M., Owens R.T., Danthuluri S.,
RA Bice T., Hoeoek M., Narayana S.V.;
RT "Novel fold and assembly of the repetitive B region of the Staphylococcus
RT aureus collagen-binding surface protein.";
RL Structure 8:67-78(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 30-330, REGION, AND COLLAGEN TYPE
RP I BINDING.
RX PubMed=16362049; DOI=10.1038/sj.emboj.7600888;
RA Zong Y., Xu Y., Liang X., Keene D.R., Hoeoek A., Gurusiddappa S.,
RA Hoeoek M., Narayana S.V.;
RT "A 'Collagen Hug' model for Staphylococcus aureus CNA binding to
RT collagen.";
RL EMBO J. 24:4224-4236(2005).
CC -!- FUNCTION: Collagen-binding adhesin that mediates bacterial adherence to
CC collagenous tissues such as cartilage (PubMed:8218209). Participates in
CC the infectious process by acting as a virulence factor in many
CC different animal models of staphylococcal infections including
CC arthritis, endocarditis and keratitis (PubMed:10816547,
CC PubMed:15181582). Inhibits the activation of the classical complement
CC pathway by interacting with host C1q and interfering with the
CC association between host C1r with C1q (PubMed:23720782).
CC {ECO:0000269|PubMed:10816547, ECO:0000269|PubMed:15181582,
CC ECO:0000269|PubMed:23720782, ECO:0000269|PubMed:8218209}.
CC -!- SUBUNIT: Interacts (via N-terminus) with type I collagen
CC (PubMed:16362049). Interacts with host C1QA (PubMed:23720782).
CC {ECO:0000269|PubMed:16362049, ECO:0000269|PubMed:23720782}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-
CC anchor {ECO:0000305}.
CC -!- DOMAIN: Composed of a N-terminal A-region and a number of B-repeats
CC depending on the strain. At the C-terminal end are features required
CC for surface targeting and covalently anchoring to the peptidoglycan.
CC The collagen binding activity is located in the A-region.
CC {ECO:0000269|PubMed:10673425, ECO:0000269|PubMed:16362049,
CC ECO:0000269|PubMed:8218209}.
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DR EMBL; M81736; AAA20874.1; -; Genomic_DNA.
DR PDB; 1AMX; X-ray; 2.00 A; A=151-318.
DR PDB; 1D2O; X-ray; 2.00 A; A/B=533-719.
DR PDB; 1D2P; X-ray; 2.50 A; A=533-905.
DR PDB; 2F68; X-ray; 1.95 A; X=30-334.
DR PDB; 2F6A; X-ray; 3.29 A; A/B/C/D=30-330.
DR PDBsum; 1AMX; -.
DR PDBsum; 1D2O; -.
DR PDBsum; 1D2P; -.
DR PDBsum; 2F68; -.
DR PDBsum; 2F6A; -.
DR AlphaFoldDB; Q53654; -.
DR SMR; Q53654; -.
DR EvolutionaryTrace; Q53654; -.
DR PRO; PR:Q53654; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:CACAO.
DR GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00222; CollagenBindB; 6.
DR DisProt; DP00098; -.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1280; -; 1.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR008454; Collagen-bd_Cna-like_B-typ_dom.
DR InterPro; IPR008456; Collagen-bd_dom.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR041033; Prealbumin-like.
DR Pfam; PF05738; Cna_B; 7.
DR Pfam; PF05737; Collagen_bind; 1.
DR Pfam; PF17802; SpaA; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Isopeptide bond; Peptidoglycan-anchor; Repeat;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1154
FT /note="Collagen adhesin"
FT /id="PRO_0000005599"
FT PROPEP 1155..1183
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005600"
FT REPEAT 533..719
FT /note="B1"
FT REPEAT 720..906
FT /note="B2"
FT REPEAT 907..1093
FT /note="B3"
FT REGION 151..318
FT /note="Collagen-binding"
FT REGION 533..1093
FT /note="3 X 187 AA approximate tandem repeats"
FT REGION 1074..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1151..1155
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 1074..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 209
FT /note="Autocatalyzes isopeptide 176-293 formation"
FT /evidence="ECO:0000255"
FT SITE 601
FT /note="Autocatalyzes isopeptide 541-618 formation"
FT /evidence="ECO:0000255"
FT SITE 692
FT /note="Autocatalyzes isopeptide 631-715 formation"
FT /evidence="ECO:0000255"
FT SITE 788
FT /note="Autocatalyzes isopeptide 728-805 formation"
FT /evidence="ECO:0000255"
FT SITE 879
FT /note="Autocatalyzes isopeptide 818-902 formation"
FT /evidence="ECO:0000255"
FT SITE 975
FT /note="Autocatalyzes isopeptide 915-992 formation"
FT /evidence="ECO:0000255"
FT SITE 1066
FT /note="Autocatalyzes isopeptide 1005-1089 formation"
FT /evidence="ECO:0000255"
FT MOD_RES 1154
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CROSSLNK 176..293
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT /evidence="ECO:0000255"
FT CROSSLNK 541..618
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT /evidence="ECO:0000255"
FT CROSSLNK 631..715
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT /evidence="ECO:0000255"
FT CROSSLNK 728..805
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT /evidence="ECO:0000255"
FT CROSSLNK 818..902
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT /evidence="ECO:0000255"
FT CROSSLNK 915..992
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT /evidence="ECO:0000255"
FT CROSSLNK 1005..1089
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT /evidence="ECO:0000255"
FT MUTAGEN 175
FT /note="Y->K: More than 90% loss of collagen-binding."
FT /evidence="ECO:0000269|PubMed:16362049"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 52..65
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2F68"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 123..139
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:2F68"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1AMX"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:2F68"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:2F6A"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:2F68"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:2F68"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 273..284
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 289..299
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:2F68"
FT STRAND 534..545
FT /evidence="ECO:0007829|PDB:1D2O"
FT TURN 546..550
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 555..563
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 566..574
FT /evidence="ECO:0007829|PDB:1D2O"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 580..590
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 597..601
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 615..620
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 624..636
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 647..653
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 656..665
FT /evidence="ECO:0007829|PDB:1D2O"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 671..681
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 688..692
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 699..704
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 710..717
FT /evidence="ECO:0007829|PDB:1D2O"
FT STRAND 721..732
FT /evidence="ECO:0007829|PDB:1D2P"
FT TURN 733..737
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 744..750
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 753..760
FT /evidence="ECO:0007829|PDB:1D2P"
FT HELIX 762..764
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 766..777
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 784..788
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 794..799
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 802..807
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 811..822
FT /evidence="ECO:0007829|PDB:1D2P"
FT HELIX 823..825
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 832..840
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 843..852
FT /evidence="ECO:0007829|PDB:1D2P"
FT TURN 853..857
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 858..868
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 875..879
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 886..891
FT /evidence="ECO:0007829|PDB:1D2P"
FT HELIX 895..897
FT /evidence="ECO:0007829|PDB:1D2P"
FT STRAND 898..904
FT /evidence="ECO:0007829|PDB:1D2P"
SQ SEQUENCE 1183 AA; 133067 MW; B6A1CC072E575D76 CRC64;
MNKNVLKFMV FIMLLNIITP LFNKNEAFAA RDISSTNVTD LTVSPSKIED GGKTTVKMTF
DDKNGKIQNG DMIKVAWPTS GTVKIEGYSK TVPLTVKGEQ VGQAVITPDG ATITFNDKVE
KLSDVSGFAE FEVQGRNLTQ TNTSDDKVAT ITSGNKSTNV TVHKSEAGTS SVFYYKTGDM
LPEDTTHVRW FLNINNEKSY VSKDITIKDQ IQGGQQLDLS TLNINVTGTH SNYYSGQSAI
TDFEKAFPGS KITVDNTKNT IDVTIPQGYG SYNSFSINYK TKITNEQQKE FVNNSQAWYQ
EHGKEEVNGK SFNHTVHNIN ANAGIEGTVK GELKVLKQDK DTKAPIANVK FKLSKKDGSV
VKDNQKEIEI ITDANGIANI KALPSGDYIL KEIEAPRPYT FDKDKEYPFT MKDTDNQGYF
TTIENAKAIE KTKDVSAQKV WEGTQKVKPT IYFKLYKQDD NQNTTPVDKA EIKKLEDGTT
KVTWSNLPEN DKNGKAIKYL VKEVNAQGED TTPEGYTKKE NGLVVTNTEK PIETTSISGE
KVWDDKDNQD GKRPEKVSVN LLANGEKVKT LDVTSETNWK YEFKDLPKYD EGKKIEYTVT
EDHVKDYTTD INGTTITNKY TPGETSATVT KNWDDNNNQD GKRPTEIKVE LYQDGKATGK
TAILNESNNW THTWTGLDEK AKGQQVKYTV EELTKVKGYT THVDNNDMGN LIVTNKYTPE
TTSISGEKVW DDKDNQDGKR PEKVSVNLLA DGEKVKTLDV TSETNWKYEF KDLPKYDEGK
KIEYTVTEDH VKDYTTDING TTITNKYTPG ETSATVTKNW DDNNNQDGKR PTEIKVELYQ
DGKATGKTAI LNESNNWTHT WTGLDEKAKG QQVKYTVEEL TKVKGYTTHV DNNDMGNLIV
TNKYTPETTS ISGEKVWDDK DNQDGKRPEK VSVNLLANGE KVKTLDVTSE TNWKYEFKDL
PKYDEGKKIE YTVTEDHVKD YTTDINGTTI TNKYTPGETS ATVTKNWDDN NNQDGKRPTE
IKVELYQDGK ATGKTAILNE SNNWTHTWTG LDEKAKGQQV KYTVDELTKV NGYTTHVDNN
DMGNLIVTNK YTPKKPNKPI YPEKPKDKTP PTKPDHSNKV KPTPPDKPSK VDKDDQPKDN
KTKPENPLKE LPKTGMKIIT SWITWVFIGI LGLYLILRKR FNS
