SDRC_STAA3
ID SDRC_STAA3 Reviewed; 947 AA.
AC Q2FJ79;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Serine-aspartate repeat-containing protein C;
DE Flags: Precursor;
GN Name=sdrC; OrderedLocusNames=SAUSA300_0546;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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; CP000255; ABD21592.1; -; Genomic_DNA.
DR RefSeq; WP_001060483.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FJ79; -.
DR SMR; Q2FJ79; -.
DR PRIDE; Q2FJ79; -.
DR EnsemblBacteria; ABD21592; ABD21592; SAUSA300_0546.
DR KEGG; saa:SAUSA300_0546; -.
DR HOGENOM; CLU_004137_1_2_9; -.
DR OMA; KGHVNST; -.
DR PRO; PR:Q2FJ79; -.
DR Proteomes; UP000001939; 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..913
FT /note="Serine-aspartate repeat-containing protein C"
FT /id="PRO_0000281386"
FT PROPEP 914..947
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000281387"
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 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"
SQ SEQUENCE 947 AA; 102928 MW; 75A53A774D02923E CRC64;
MNNKKTATNR KGMIPNRLNK FSIRKYSVGT ASILVGTTLI FGLSGHEAKA AEHTNGELNQ
SKNETTAPSE NKTTKKVDSR QLKDNTQTAT ADQPKVTMSD SATVKETSSN MQSPQNATAN
QSTTKTSNVT TNDKSSTTYS NETDKSNLTQ AKDVSTTPKT TTIKPRTLNR MAVNTVAAPQ
QGTNVNDKVH FSNIDIAIDK GHVNQTTGKT EFWATSSDVL KLKANYTIDD SVKEGDIFTF
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 DSDSDSDSDS DSDSDSDSDS DSDSDNDSDS DSDSDSDAGK HTPAKPMSTV
KDQHKTAKAL PETGSENNNS NNGTLFGGLF AALGSLLLFG RRKKQNK
