SDRC_STAAE
ID SDRC_STAAE Reviewed; 947 AA.
AC O86487; A6QEL3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Serine-aspartate repeat-containing protein C;
DE Flags: Precursor;
GN Name=sdrC; OrderedLocusNames=NWMN_0523;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9884231; DOI=10.1099/00221287-144-12-3387;
RA Josefsson E., McCrea K.W., Eidhin D.N., O'Connell D., Cox J.A., Hoeoek M.,
RA Foster T.J.;
RT "Three new members of the serine-aspartate repeat protein multigene family
RT of Staphylococcus aureus.";
RL Microbiology 144:3387-3395(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [3]
RP FUNCTION, AND INTERACTION WITH HOST NRXN1.
RC STRAIN=Newman;
RX PubMed=20090838; DOI=10.1371/journal.ppat.1000726;
RA Barbu E.M., Ganesh V.K., Gurusiddappa S., Mackenzie R.C., Foster T.J.,
RA Sudhof T.C., Hoeoek M.;
RT "beta-Neurexin is a ligand for the Staphylococcus aureus MSCRAMM SdrC.";
RL PLoS Pathog. 6:E1000726-E1000726(2010).
RN [4]
RP SUBUNIT.
RC STRAIN=Newman;
RX PubMed=25115812; DOI=10.1111/mmi.12750;
RA Barbu E.M., Mackenzie C., Foster T.J., Hoeoek M.;
RT "SdrC induces staphylococcal biofilm formation through a homophilic
RT interaction.";
RL Mol. Microbiol. 94:172-185(2014).
RN [5]
RP FUNCTION.
RX PubMed=28320940; DOI=10.1073/pnas.1616805114;
RA Feuillie C., Formosa-Dague C., Hays L.M., Vervaeck O., Derclaye S.,
RA Brennan M.P., Foster T.J., Geoghegan J.A., Dufrene Y.F.;
RT "Molecular interactions and inhibition of the staphylococcal biofilm-
RT forming protein SdrC.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:3738-3743(2017).
CC -!- FUNCTION: Cell surface-associated calcium-binding protein which plays
CC an important role in adhesion and pathogenesis (PubMed:20090838,
CC PubMed:9884231, PubMed:28320940). Mediates interactions with components
CC of the extracellular matrix such as host NRXN1 to promote bacterial
CC adhesion (PubMed:20090838). {ECO:0000269|PubMed:20090838,
CC ECO:0000269|PubMed:28320940, ECO:0000269|PubMed:9884231}.
CC -!- SUBUNIT: Homodimerizes; via N2-Domain (PubMed:25115812). Interacts with
CC host NRXN1; this interaction mediates bacterial attachment to host
CC cells (PubMed:20090838). {ECO:0000269|PubMed:20090838,
CC ECO:0000269|PubMed:25115812}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}. Note=Anchored to the cell wall by sortase A.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ005645; CAA06650.1; -; Genomic_DNA.
DR EMBL; AP009351; BAF66795.1; -; Genomic_DNA.
DR RefSeq; WP_001060502.1; NZ_CP023390.1.
DR AlphaFoldDB; O86487; -.
DR SMR; O86487; -.
DR EnsemblBacteria; BAF66795; BAF66795; NWMN_0523.
DR KEGG; sae:NWMN_0523; -.
DR HOGENOM; CLU_004137_1_2_9; -.
DR OMA; KGHVNST; -.
DR PRO; PR:O86487; -.
DR Proteomes; UP000006386; 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 Calcium; Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..913
FT /note="Serine-aspartate repeat-containing protein C"
FT /id="PRO_0000280233"
FT PROPEP 914..947
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000280234"
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..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 21..32
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000250|UniProtKB:Q2G0L5"
FT MOTIF 910..914
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..882
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 913
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 938
FT /note="L -> S (in Ref. 1; CAA06650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 947 AA; 102915 MW; 3C765E6E35121554 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 DSDSDSNSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDNDSDS DSDSDSDAGK HTPAKPMSTV
KDQHKTAKAL PETGSENNNS NNGTLFGGLF AALGSLLLFG RRKKQNK
