SDRC_STAA8
ID SDRC_STAA8 Reviewed; 995 AA.
AC Q2G0L5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Serine-aspartate repeat-containing protein C;
DE Flags: Precursor;
GN Name=sdrC; OrderedLocusNames=SAOUHSC_00544;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP SUBCELLULAR LOCATION.
RC STRAIN=RN4220;
RX PubMed=18800056; DOI=10.1038/emboj.2008.185;
RA DeDent A., Bae T., Missiakas D.M., Schneewind O.;
RT "Signal peptides direct surface proteins to two distinct envelope locations
RT of Staphylococcus aureus.";
RL EMBO J. 27:2656-2668(2008).
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, ECO:0000269|PubMed:18800056}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477}. Note=Found in a ring-like
CC distribution on the cell surface (PubMed:18800056). Anchored to the
CC cell wall by sortase A (Probable). {ECO:0000269|PubMed:18800056,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; CP000253; ABD29692.1; -; Genomic_DNA.
DR RefSeq; WP_001060498.1; NZ_LS483365.1.
DR RefSeq; YP_499117.1; NC_007795.1.
DR PDB; 6LXH; X-ray; 2.07 A; A/B/C=178-496.
DR PDB; 6LXS; X-ray; 1.58 A; A=178-496.
DR PDBsum; 6LXH; -.
DR PDBsum; 6LXS; -.
DR AlphaFoldDB; Q2G0L5; -.
DR SMR; Q2G0L5; -.
DR STRING; 1280.SAXN108_0617; -.
DR EnsemblBacteria; ABD29692; ABD29692; SAOUHSC_00544.
DR GeneID; 3920824; -.
DR KEGG; sao:SAOUHSC_00544; -.
DR PATRIC; fig|93061.5.peg.490; -.
DR eggNOG; COG3266; Bacteria.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_004137_1_2_9; -.
DR OMA; KGHVNST; -.
DR PRO; PR:Q2G0L5; -.
DR Proteomes; UP000008816; 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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell wall; Peptidoglycan-anchor; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..961
FT /note="Serine-aspartate repeat-containing protein C"
FT /id="PRO_0000281388"
FT PROPEP 962..995
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000281389"
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..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 21..32
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000305|PubMed:18800056"
FT MOTIF 958..962
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..164
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..930
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 961
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:6LXS"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6LXS"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:6LXH"
FT STRAND 219..228
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:6LXS"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:6LXS"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 295..304
FT /evidence="ECO:0007829|PDB:6LXS"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 314..322
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 325..334
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:6LXS"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 373..383
FT /evidence="ECO:0007829|PDB:6LXS"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:6LXS"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6LXS"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:6LXS"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6LXS"
FT TURN 426..429
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:6LXS"
FT TURN 435..438
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 446..455
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 463..472
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 474..484
FT /evidence="ECO:0007829|PDB:6LXS"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:6LXS"
SQ SEQUENCE 995 AA; 107795 MW; 3F3EF59667FB8039 CRC64;
MNNKKTATNR KGMIPNRLNK FSIRKYSVGT ASILVGTTLI FGLSGHEAKA AEHTNGELNQ
SKNETTAPSE NKTTKKVDSR QLKDNTQTAT ADQPKVTMSD SATVKETSSN MQSPQNATAN
QSTTKTSNVT TNDKSSTTYS NETDKSNLTQ AKDVSTTPKT TTIKPRTLNR MAVNTVAAPQ
QGTNVNDKVH FSNIDIAIDK GHVNQTTGKT EFWATSSDVL KLKANYTIDD SVKEGDTFTF
KYGQYFRPGS VRLPSQTQNL YNAQGNIIAK GIYDSTTNTT TYTFTNYVDQ YTNVRGSFEQ
VAFAKRKNAT TDKTAYKMEV TLGNDTYSEE IIVDYGNKKA QPLISSTNYI NNEDLSRNMT
AYVNQPKNTY TKQTFVTNLT GYKFNPNAKN FKIYEVTDQN QFVDSFTPDT SKLKDVTDQF
DVIYSNDNKT ATVDLMKGQT SSNKQYIIQQ VAYPDNSSTD NGKIDYTLDT DKTKYSWSNS
YSNVNGSSTA NGDQKKYNLG DYVWEDTNKD GKQDANEKGI KGVYVILKDS NGKELDRTTT
DENGKYQFTG LSNGTYSVEF STPAGYTPTT ANVGTDDAVD 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 DSDSDSDSDS
DSDSDSDSDS DSDSDSDNDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDNDSDSDS DSDSDAGKHT PAKPMSTVKD QHKTAKALPE
TGSENNNSNN GTLFGGLFAA LGSLLLFGRR KKQNK
