SDRC_STAAC
ID SDRC_STAAC Reviewed; 947 AA.
AC Q5HIB4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Serine-aspartate repeat-containing protein C;
DE Flags: Precursor;
GN Name=sdrC; OrderedLocusNames=SACOL0608;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW37717.1; -; Genomic_DNA.
DR RefSeq; WP_001060500.1; NC_002951.2.
DR AlphaFoldDB; Q5HIB4; -.
DR SMR; Q5HIB4; -.
DR EnsemblBacteria; AAW37717; AAW37717; SACOL0608.
DR KEGG; sac:SACOL0608; -.
DR HOGENOM; CLU_004137_1_2_9; -.
DR OMA; KGHVNST; -.
DR PRO; PR:Q5HIB4; -.
DR Proteomes; UP000000530; 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_0000281390"
FT PROPEP 914..947
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000281391"
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; 102916 MW; 389C5E6432A97F5E 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 DSDSDSDSDS DSDSDSDSDS DSDSDNDSDS DSDSDSDAGK HTPAKPMSTV
KDQHKTAKAL PETGSENNNS NNGTLFGGLF AALGSLLLFG RRKKQNK
