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SDRC_STAAN
ID   SDRC_STAAN              Reviewed;         953 AA.
AC   Q7A781;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, 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=SA0519;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB41750.1; -; Genomic_DNA.
DR   PIR; C89824; C89824.
DR   RefSeq; WP_001060462.1; NC_002745.2.
DR   AlphaFoldDB; Q7A781; -.
DR   SMR; Q7A781; -.
DR   EnsemblBacteria; BAB41750; BAB41750; BAB41750.
DR   KEGG; sau:SA0519; -.
DR   HOGENOM; CLU_004137_1_2_9; -.
DR   OMA; KGHVNST; -.
DR   PRO; PR:Q7A781; -.
DR   Proteomes; UP000000751; 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..919
FT                   /note="Serine-aspartate repeat-containing protein C"
FT                   /id="PRO_0000281394"
FT   PROPEP          920..953
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000281395"
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..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           916..920
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..160
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..888
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         919
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   953 AA;  103293 MW;  729A7169A074A1E5 CRC64;
     MNNKKTATNR KGMIPNRLNK FSIRKYSVGT ASILVGTTLI FGLSGHEAKA AEHTNGELNQ
     SKNETTAPSE NKTTEKVDSR QLKDNTQTAT ADQPKVTMSD SATVKETSSN MQSPQNATAS
     QSTTQTSNVT TNDKSSTTYS NETDKSNLTQ AKNVSTTPKT TTIKQRALNR MAVNTVAAPQ
     QGTNVNDKVH FTNIDIAIDK GHVNKTTGNT EFWATSSDVL KLKANYTIDD SVKEGDTFTF
     KYGQYFRPGS VRLPSQTQNL YNAQGNIIAK GIYDSKTNTT TYTFTNYVDQ YTNVSGSFEQ
     VAFAKRENAT TDKTAYKMEV TLGNDTYSKD VIVDYGNQKG QQLISSTNYI NNEDLSRNMT
     VYVNQPKKTY TKETFVTNLT GYKFNPDAKN FKIYEVTDQN QFVDSFTPDT SKLKDVTGQF
     DVIYSNDNKT ATVDLLNGQS SSDKQYIIQQ VAYPDNSSTD NGKIDYTLET QNGKSSWSNS
     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 DSESDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDNDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDAGKHTPT
     KPMSTVKDQH KTAKALPETG SENNNSNNGT LFGGLFAALG SLLLFGRRKK QNK
 
 
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