ID   Y497_RICCN              Reviewed;         267 AA.
AC   Q92IC3;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Putative N-acetylmuramoyl-L-alanine amidase RC0497;
DE            EC=3.5.1.28;
GN   OrderedLocusNames=RC0497;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AE006914; AAL03035.1; -; Genomic_DNA.
DR   PIR; A97762; A97762.
DR   RefSeq; WP_004995964.1; NC_003103.1.
DR   AlphaFoldDB; Q92IC3; -.
DR   SMR; Q92IC3; -.
DR   EnsemblBacteria; AAL03035; AAL03035; RC0497.
DR   KEGG; rco:RC0497; -.
DR   HOGENOM; CLU_092794_0_0_5; -.
DR   OMA; ISWTEAG; -.
DR   BRENDA; 3.5.1.28; 5446.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 1.10.101.10; -; 1.
DR   Gene3D; 3.40.80.10; -; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SUPFAM; SSF47090; SSF47090; 1.
DR   SUPFAM; SSF55846; SSF55846; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Secreted.
FT   CHAIN           1..267
FT                   /note="Putative N-acetylmuramoyl-L-alanine amidase RC0497"
FT                   /id="PRO_0000279758"
FT   DOMAIN          33..141
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   267 AA;  29592 MW;  F936FEBF70E673F3 CRC64;
     MSKSKAIENN GISNTNSPNG KYMAPRPEGV KPTCVVITYS VSKDIKAVRE VLDERGASVH
     YIIDKDGTQK EYHNDLTDQA FYAGKSSWKG EVGVNKFGIG VMLINDAKSD FPAEQIGKLK
     EFLKDVTERY PNLDLKHDLV GLGEVTVNRE GNAHIAPGSK FPWKELAEAG FGRYFETTQE
     QKSKLLLSLD STGEKVNTLQ ENLKEYGYGV ESTSTFDQFT QQAVRVFNDR YGTGLPNEEP
     PVSWTEAGQD VLSQLLGQTV LEQTENA