SDRC_STAAW
ID SDRC_STAAW Reviewed; 955 AA.
AC Q8NXX7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Serine-aspartate repeat-containing protein C;
DE Flags: Precursor;
GN Name=sdrC; OrderedLocusNames=MW0516;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB94381.1; -; Genomic_DNA.
DR RefSeq; WP_001060526.1; NC_003923.1.
DR AlphaFoldDB; Q8NXX7; -.
DR SMR; Q8NXX7; -.
DR EnsemblBacteria; BAB94381; BAB94381; BAB94381.
DR KEGG; sam:MW0516; -.
DR HOGENOM; CLU_004137_1_1_9; -.
DR OMA; KGHVNST; -.
DR PRO; PR:Q8NXX7; -.
DR Proteomes; UP000000418; 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..921
FT /note="Serine-aspartate repeat-containing protein C"
FT /id="PRO_0000281400"
FT PROPEP 922..955
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000281401"
FT DOMAIN 496..606
FT /note="CNA-B 1"
FT DOMAIN 607..717
FT /note="CNA-B 2"
FT REGION 51..495
FT /note="Ligand binding A region"
FT REGION 51..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 918..922
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 83..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..890
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 921
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 955 AA; 103642 MW; 65FD8BB93A477A22 CRC64;
MNNKKTVTNR KGMIPNRLNK FSIRKYSVGT ASILVGTTLI FGLSGHEAKA AEHTNGELNQ
SKNETTAPSE NKTTEKVDSH QLKDNTQTAT ADQPKVTMSD SATFKETSSN MQSPQNATAS
QSTTQTSNVT TNDKSSTTYS NETDKSNLTQ AKDVSATPKT TTIKPRTLNR MAVNTVAAPQ
QGTNVNDKVH FSNIDIAIDK GHLNKDTGKT EFWATSSDVL KLKANYTIDD SVKEGDTFTF
KYGQYFRPGS VRLPSQTQNL YNAQGNIIAK GIYDSTTNTT TYTFTNYVDQ YTNVSGSFEQ
VAFAKRENAT TDKTAYKMEV SLGNDTYSEE IIVDYGNKKA QPLISSTNYI NNEDLSRNMT
AYVNQPKNTY TKQTFVTNLT GYKFNPNAKN FKIYEVTDQN QFVDSFTPDT SKLKDVTNQF
NITYSNDNKT ATVDLMNGQT SSNKQYIIQQ VAYPDNTSTD NGKIDYTLDT DKTKYSWSNS
YSNVNGSSTA NGDQKKYNLG DYVWEDTNKD GKQDANEKGI KGVYVILKDS NGKELDRTTT
DENGKYQFTG LSNGTYSVEF STPAGYTPTT ANAGTDDAVD SDGLTTTGVI KDADNMTLDS
GFYKTPKYSL GDYVWYDSNK DGKQDSTEKG IKGVKVTLQN EKGEVIGTTE TDENGKYRFD
NLDSGKYKVI FEKPAGLTQT GTNTTEDDKD ADGGEVDVTI TDHDDFTLDN GYYEEETSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DTDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSESDADSDT DSDSDAGKHT
PAKPMSTVKD QHKTAKALPE TGSENNNSNN GTLFGGLFAA LGSLLLFGRR KKQNK
