SDRC_STAAR
ID SDRC_STAAR Reviewed; 906 AA.
AC Q6GJA7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Serine-aspartate repeat-containing protein C;
DE Flags: Precursor;
GN Name=sdrC; OrderedLocusNames=SAR0566;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Cell surface-associated calcium-binding protein which plays
CC an important role in adhesion and pathogenesis. Mediates interactions
CC with components of the extracellular matrix such as host NRXN1 to
CC promote bacterial adhesion. {ECO:0000250|UniProtKB:O86487}.
CC -!- SUBUNIT: Homodimerizes; via N2-Domain. Interacts with host NRXN1; this
CC interaction mediates bacterial attachment to host cells.
CC {ECO:0000250|UniProtKB:O86487}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; BX571856; CAG39587.1; -; Genomic_DNA.
DR RefSeq; WP_001060422.1; NC_002952.2.
DR AlphaFoldDB; Q6GJA7; -.
DR SMR; Q6GJA7; -.
DR KEGG; sar:SAR0566; -.
DR HOGENOM; CLU_004137_1_2_9; -.
DR OMA; KGHVNST; -.
DR OrthoDB; 58491at2; -.
DR PRO; PR:Q6GJA7; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.1280; -; 1.
DR InterPro; IPR011266; Adhesin_Fg-bd_dom_2.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR033764; Sdr_B.
DR InterPro; IPR041171; SDR_Ig.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF17210; SdrD_B; 2.
DR Pfam; PF10425; SdrG_C_C; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Calcium; Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..872
FT /note="Serine-aspartate repeat-containing protein C"
FT /id="PRO_0000281396"
FT PROPEP 873..906
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000281397"
FT DOMAIN 487..597
FT /note="CNA-B 1"
FT DOMAIN 598..708
FT /note="CNA-B 2"
FT REGION 51..486
FT /note="Ligand binding A region"
FT REGION 51..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 869..873
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..841
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 872
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 906 AA; 98608 MW; 63511E8951469C29 CRC64;
MNNKKTATNR KGMIPNRLNK FSIRKYSVGT ASILVGTTLI FGLSGHEAKA AEHTNGELNQ
SKNEATAPSE NKTTEKVDSR QQNNVEQSTT SNQPKVNESD NTSVKETTEE PQNTTSTQPT
KKNNDATANK DNLAAQNIST QANDVSATPK TTTIKPRTLN RMAVNTVAAP QQGTNVNDKV
HFSNIDIAID KGHVNSTTGK TEFWATSSDV LKLKANYTID DSVKEGDTFT FKYGQYFRPG
SVRLPSQTQN LYNAQGNIIA KGIYDSTTNT TTYTFTNYVD QYTNVSGSFE QVAFAKRENA
TTDKTAYKME VTLGNDAYSE EIIVDYGNKK AQPLISSTNY INNEDLSRNM TVYVNQPKNT
YTKETFVSTL TGYKFNPDAK NFKIYEVTDQ NQFVDSFTPD TSKLIDVTDK FKITYSNDNK
TATVDLMNGQ TNSNKQYIIQ QVAYPDNTST DNGKIDYTLD TDKTKYSWSN SYSSVNGSST
ANGDQKKYNL GDYVWEDTNK DGKQDANEKG IKGVYVILKD SNGKELDRTT TDENGKYQFT
GLGNGTYSVE FSTLAGYTPT TVNAGTDDAV DSDGLTTTGV IKDADNMTLD SGFYKTPKYS
LGDYVWYDSN KDGKQDSTEK GIKGVKVTLQ NEKGEVIGTT ETDENGKYRF DNLDSGKYKV
IFEKPAGLKQ TGTNTTEDDK DADGGEVDVT ITDHDDFTLD NGYFEEETSD SDSDSDSDSD
SDSDSDSDSD SDSESDSDSD SDSDSDSDSD SDSDSDSDSD SESDSDSDSD SDSDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
SDSDSDAGKH TPVKPMSATK DHHNKAKALP ETGSENNGSN NATLFGGLFA ALGSLLLFGR
RKKQNK
