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Y2979_STAA8
ID   Y2979_STAA8             Reviewed;         619 AA.
AC   Q2G222;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979;
DE   Flags: Precursor;
GN   OrderedLocusNames=SAOUHSC_02979;
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   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=ISP479C;
RX   PubMed=18621893; DOI=10.1128/jb.00300-08;
RA   Siboo I.R., Chaffin D.O., Rubens C.E., Sullam P.M.;
RT   "Characterization of the accessory Sec system of Staphylococcus aureus.";
RL   J. Bacteriol. 190:6188-6196(2008).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=RN4220;
RX   PubMed=20472795; DOI=10.1128/jb.01452-09;
RA   Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E.,
RA   Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S.,
RA   van Dijl J.M.;
RT   "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in
RT   Staphylococcus aureus.";
RL   J. Bacteriol. 192:3788-3800(2010).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18621893,
CC       ECO:0000269|PubMed:20472795}.
CC   -!- INDUCTION: More protein is secreted in a secA2 mutant
CC       (PubMed:18621893), while less protein is secreted in a secG or double
CC       secG/secY2 mutant (PubMed:20472795) (at protein level).
CC       {ECO:0000269|PubMed:18621893, ECO:0000269|PubMed:20472795}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the N-acetylmuramoyl-
CC       L-alanine amidase 2 family. {ECO:0000305}.
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DR   EMBL; CP000253; ABD31967.1; -; Genomic_DNA.
DR   RefSeq; WP_001125611.1; NZ_LS483365.1.
DR   RefSeq; YP_501429.1; NC_007795.1.
DR   PDB; 5T1Q; X-ray; 2.15 A; A/B/C/D=261-619.
DR   PDBsum; 5T1Q; -.
DR   AlphaFoldDB; Q2G222; -.
DR   SMR; Q2G222; -.
DR   STRING; 1280.SAXN108_2915; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   PRIDE; Q2G222; -.
DR   EnsemblBacteria; ABD31967; ABD31967; SAOUHSC_02979.
DR   GeneID; 3921462; -.
DR   KEGG; sao:SAOUHSC_02979; -.
DR   PATRIC; fig|93061.5.peg.2687; -.
DR   eggNOG; COG1705; Bacteria.
DR   eggNOG; COG3942; Bacteria.
DR   HOGENOM; CLU_017855_1_0_9; -.
DR   OMA; YNRMAQF; -.
DR   PRO; PR:Q2G222; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   InterPro; IPR007921; CHAP_dom.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   Pfam; PF05257; CHAP; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   SMART; SM00047; LYZ2; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50911; CHAP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..619
FT                   /note="N-acetylmuramoyl-L-alanine amidase domain-containing
FT                   protein SAOUHSC_02979"
FT                   /id="PRO_0000414194"
FT   DOMAIN          488..617
FT                   /note="Peptidase C51"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
FT   REGION          25..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..468
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT   COMPBIAS        35..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           269..273
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          284..286
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           288..290
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          297..299
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          312..314
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           318..338
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           342..353
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   TURN            354..357
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   TURN            359..361
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   TURN            363..365
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          378..388
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          391..400
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           405..418
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   TURN            424..427
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           428..430
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   TURN            432..434
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           438..445
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   TURN            446..449
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           455..465
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           468..471
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          473..475
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           479..481
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           482..485
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           513..522
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   TURN            523..525
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           535..537
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           538..544
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          548..552
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          558..561
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           565..567
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   TURN            570..572
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          574..581
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          587..596
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          599..605
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   HELIX           607..610
FT                   /evidence="ECO:0007829|PDB:5T1Q"
FT   STRAND          613..617
FT                   /evidence="ECO:0007829|PDB:5T1Q"
SQ   SEQUENCE   619 AA;  69253 MW;  36FABFC6B73AF256 CRC64;
     MPKNKILIYL LSTTLVLPTL VSPTAYADTP QKDTTAKTTS HDSKKSNDDE TSKDTTSKDI
     DKADKNNTSN QDNNDKKFKT IDDSTSDSNN IIDFIYKNLP QTNINQLLTK NKYDDNYSLT
     TLIQNLFNLN SDISDYEQPR NGEKSTNDSN KNSDNSIKND TDTQSSKQDK ADNQKAPKSN
     NTKPSTSNKQ PNSPKPTQPN QSNSQPASDD KANQKSSSKD NQSMSDSALD SILDQYSEDA
     KKTQKDYASQ SKKDKNEKSN TKNPQLPTQD ELKHKSKPAQ SFNNDVNQKD TRATSLFETD
     PSISNNDDSG QFNVVDSKDT RQFVKSIAKD AHRIGQDNDI YASVMIAQAI LESDSGRSAL
     AKSPNHNLFG IKGAFEGNSV PFNTLEADGN QLYSINAGFR KYPSTKESLK DYSDLIKNGI
     DGNRTIYKPT WKSEADSYKD ATSHLSKTYA TDPNYAKKLN SIIKHYQLTQ FDDERMPDLD
     KYERSIKDYD DSSDEFKPFR EVSDSMPYPH GQCTWYVYNR MKQFGTSISG DLGDAHNWNN
     RAQYRDYQVS HTPKRHAAVV FEAGQFGADQ HYGHVAFVEK VNSDGSIVIS ESNVKGLGII
     SHRTINAAAA EELSYITGK
 
 
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