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Collagen adhesin

 CNA_STAAU               Reviewed;        1183 AA.
Q53654;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 107.
RecName: Full=Collagen adhesin;
Flags: Precursor;
Name=cna;
Staphylococcus aureus.
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=1280;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=FDA 574;
PubMed=1311320;
Patti J.M., Jonsson H., Guss B., Switalski L.M., Wiberg K.,
Lindberg M., Hoeoek M.;
"Molecular characterization and expression of a gene encoding a
Staphylococcus aureus collagen adhesin.";
J. Biol. Chem. 267:4766-4772(1992).
[2]
ERRATUM.
Patti J.M., Jonsson H., Guss B., Switalski L.M., Wiberg K.,
Lindberg M., Hoeoek M.;
J. Biol. Chem. 269:11672-11672(1994).
[3]
DOMAIN COLLAGEN-BINDING.
STRAIN=FDA 574;
PubMed=8218209; DOI=10.1021/bi00093a021;
Patti J.M., Boles J.O., Hoeoek M.;
"Identification and biochemical characterization of the ligand binding
domain of the collagen adhesin from Staphylococcus aureus.";
Biochemistry 32:11428-11435(1993).
[4]
CROSS-LINKS.
PubMed=18063798; DOI=10.1126/science.1145806;
Kang H.J., Coulibaly F., Clow F., Proft T., Baker E.N.;
"Stabilizing isopeptide bonds revealed in Gram-positive bacterial
pilus structure.";
Science 318:1625-1628(2007).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 169-318.
PubMed=9334749; DOI=10.1038/nsb1097-833;
Symersky J., Patti J.M., Carson M., House-Pompeo K., Teale M.,
Moore D., Jin L., Schneider A., DeLucas L.J., Hoeoek M.,
Narayana S.V.L.;
"Structure of the collagen-binding domain from a Staphylococcus aureus
adhesin.";
Nat. Struct. Biol. 4:833-838(1997).
-!- FUNCTION: Mediates attachment of staphylococcal cells to collagen-
containing substrata.
-!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305};
Peptidoglycan-anchor {ECO:0000305}.
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EMBL; M81736; AAA20874.1; -; Genomic_DNA.
PDB; 1AMX; X-ray; 2.00 A; A=151-318.
PDB; 1D2O; X-ray; 2.00 A; A/B=533-719.
PDB; 1D2P; X-ray; 2.50 A; A=533-905.
PDB; 2F68; X-ray; 1.95 A; X=30-334.
PDB; 2F6A; X-ray; 3.29 A; A/B/C/D=30-330.
PDBsum; 1AMX; -.
PDBsum; 1D2O; -.
PDBsum; 1D2P; -.
PDBsum; 2F68; -.
PDBsum; 2F6A; -.
DisProt; DP00098; -.
ProteinModelPortal; Q53654; -.
SMR; Q53654; -.
PRIDE; Q53654; -.
EvolutionaryTrace; Q53654; -.
PRO; PR:Q53654; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:CACAO.
GO; GO:0005518; F:collagen binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
CDD; cd00222; CollagenBindB; 6.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 2.60.40.1280; -; 1.
InterPro; IPR008966; Adhesion_dom_sf.
InterPro; IPR008454; Collagen-bd_Cna-like_B-typ_dom.
InterPro; IPR008456; Collagen-bd_dom.
InterPro; IPR011252; Fibrogen-bd_dom1.
InterPro; IPR013783; Ig-like_fold.
Pfam; PF05738; Cna_B; 7.
Pfam; PF05737; Collagen_bind; 1.
SUPFAM; SSF49401; SSF49401; 2.
1: Evidence at protein level;
3D-structure; Cell wall; Isopeptide bond; Peptidoglycan-anchor;
Repeat; Secreted; Signal.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 1154 Collagen adhesin.
/FTId=PRO_0000005599.
PROPEP 1155 1183 Removed by sortase. {ECO:0000255}.
/FTId=PRO_0000005600.
REPEAT 533 719 B1.
REPEAT 720 906 B2.
REPEAT 907 1093 B3.
REGION 151 318 Collagen-binding.
REGION 533 1093 3 X 187 AA approximate tandem repeats.
MOTIF 1151 1155 LPXTG sorting signal. {ECO:0000255}.
COMPBIAS 1093 1157 Lys/Pro-rich.
SITE 209 209 Autocatalyzes isopeptide 176-293
formation. {ECO:0000255}.
SITE 601 601 Autocatalyzes isopeptide 541-618
formation. {ECO:0000255}.
SITE 692 692 Autocatalyzes isopeptide 631-715
formation. {ECO:0000255}.
SITE 788 788 Autocatalyzes isopeptide 728-805
formation. {ECO:0000255}.
SITE 879 879 Autocatalyzes isopeptide 818-902
formation. {ECO:0000255}.
SITE 975 975 Autocatalyzes isopeptide 915-992
formation. {ECO:0000255}.
SITE 1066 1066 Autocatalyzes isopeptide 1005-1089
formation. {ECO:0000255}.
MOD_RES 1154 1154 Pentaglycyl murein peptidoglycan amidated
threonine. {ECO:0000255}.
CROSSLNK 176 293 Isoaspartyl lysine isopeptide (Lys-Asn).
{ECO:0000255}.
CROSSLNK 541 618 Isoaspartyl lysine isopeptide (Lys-Asn).
{ECO:0000255}.
CROSSLNK 631 715 Isoaspartyl lysine isopeptide (Lys-Asn).
{ECO:0000255}.
CROSSLNK 728 805 Isoaspartyl lysine isopeptide (Lys-Asn).
{ECO:0000255}.
CROSSLNK 818 902 Isoaspartyl lysine isopeptide (Lys-Asn).
{ECO:0000255}.
CROSSLNK 915 992 Isoaspartyl lysine isopeptide (Lys-Asn).
{ECO:0000255}.
CROSSLNK 1005 1089 Isoaspartyl lysine isopeptide (Lys-Asn).
{ECO:0000255}.
HELIX 34 37 {ECO:0000244|PDB:2F68}.
STRAND 38 48 {ECO:0000244|PDB:2F68}.
STRAND 52 65 {ECO:0000244|PDB:2F68}.
STRAND 71 76 {ECO:0000244|PDB:2F68}.
STRAND 80 87 {ECO:0000244|PDB:2F68}.
STRAND 90 96 {ECO:0000244|PDB:2F68}.
STRAND 99 107 {ECO:0000244|PDB:2F68}.
STRAND 110 115 {ECO:0000244|PDB:2F68}.
HELIX 117 119 {ECO:0000244|PDB:2F68}.
STRAND 123 139 {ECO:0000244|PDB:2F68}.
STRAND 148 153 {ECO:0000244|PDB:2F68}.
STRAND 156 162 {ECO:0000244|PDB:2F68}.
STRAND 175 177 {ECO:0000244|PDB:2F68}.
STRAND 185 194 {ECO:0000244|PDB:2F68}.
STRAND 201 203 {ECO:0000244|PDB:2F68}.
STRAND 205 211 {ECO:0000244|PDB:2F68}.
STRAND 215 217 {ECO:0000244|PDB:2F68}.
HELIX 219 221 {ECO:0000244|PDB:2F68}.
STRAND 224 228 {ECO:0000244|PDB:2F68}.
STRAND 232 234 {ECO:0000244|PDB:2F68}.
STRAND 236 238 {ECO:0000244|PDB:1AMX}.
HELIX 239 246 {ECO:0000244|PDB:2F68}.
TURN 247 249 {ECO:0000244|PDB:2F6A}.
STRAND 251 255 {ECO:0000244|PDB:2F68}.
TURN 256 259 {ECO:0000244|PDB:2F68}.
STRAND 260 265 {ECO:0000244|PDB:2F68}.
HELIX 267 270 {ECO:0000244|PDB:2F68}.
STRAND 273 284 {ECO:0000244|PDB:2F68}.
STRAND 289 299 {ECO:0000244|PDB:2F68}.
STRAND 307 311 {ECO:0000244|PDB:2F68}.
STRAND 314 317 {ECO:0000244|PDB:2F68}.
STRAND 321 328 {ECO:0000244|PDB:2F68}.
STRAND 534 545 {ECO:0000244|PDB:1D2O}.
TURN 546 550 {ECO:0000244|PDB:1D2O}.
STRAND 555 563 {ECO:0000244|PDB:1D2O}.
STRAND 566 574 {ECO:0000244|PDB:1D2O}.
HELIX 575 577 {ECO:0000244|PDB:1D2O}.
STRAND 580 590 {ECO:0000244|PDB:1D2O}.
STRAND 597 601 {ECO:0000244|PDB:1D2O}.
STRAND 607 612 {ECO:0000244|PDB:1D2O}.
STRAND 615 620 {ECO:0000244|PDB:1D2O}.
STRAND 624 636 {ECO:0000244|PDB:1D2O}.
STRAND 639 641 {ECO:0000244|PDB:1D2O}.
STRAND 647 653 {ECO:0000244|PDB:1D2O}.
STRAND 656 665 {ECO:0000244|PDB:1D2O}.
HELIX 666 668 {ECO:0000244|PDB:1D2O}.
STRAND 671 681 {ECO:0000244|PDB:1D2O}.
STRAND 688 692 {ECO:0000244|PDB:1D2O}.
STRAND 699 704 {ECO:0000244|PDB:1D2O}.
STRAND 710 717 {ECO:0000244|PDB:1D2O}.
STRAND 721 732 {ECO:0000244|PDB:1D2P}.
TURN 733 737 {ECO:0000244|PDB:1D2P}.
STRAND 744 750 {ECO:0000244|PDB:1D2P}.
STRAND 753 760 {ECO:0000244|PDB:1D2P}.
HELIX 762 764 {ECO:0000244|PDB:1D2P}.
STRAND 766 777 {ECO:0000244|PDB:1D2P}.
STRAND 784 788 {ECO:0000244|PDB:1D2P}.
STRAND 794 799 {ECO:0000244|PDB:1D2P}.
STRAND 802 807 {ECO:0000244|PDB:1D2P}.
STRAND 811 822 {ECO:0000244|PDB:1D2P}.
HELIX 823 825 {ECO:0000244|PDB:1D2P}.
STRAND 832 840 {ECO:0000244|PDB:1D2P}.
STRAND 843 852 {ECO:0000244|PDB:1D2P}.
TURN 853 857 {ECO:0000244|PDB:1D2P}.
STRAND 858 868 {ECO:0000244|PDB:1D2P}.
STRAND 875 879 {ECO:0000244|PDB:1D2P}.
STRAND 886 891 {ECO:0000244|PDB:1D2P}.
HELIX 895 897 {ECO:0000244|PDB:1D2P}.
STRAND 898 904 {ECO:0000244|PDB:1D2P}.
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


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