ID   Q1YLV1_AURMS            Unreviewed;       409 AA.
AC   Q1YLV1;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   13-SEP-2023, entry version 58.
DE   SubName: Full=Putative D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:EAS51630.1};
GN   ORFNames=SI859A1_02446 {ECO:0000313|EMBL:EAS51630.1};
OS   Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Aurantimonadaceae; Aurantimonas.
OX   NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS51630.1, ECO:0000313|Proteomes:UP000000321};
RN   [1] {ECO:0000313|EMBL:EAS51630.1, ECO:0000313|Proteomes:UP000000321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS51630.1,
RC   ECO:0000313|Proteomes:UP000000321};
RX   PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA   Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA   McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT   "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT   Aurantimonas sp. strain SI85-9A1.";
RL   Appl. Environ. Microbiol. 74:2646-2658(2008).
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAS51630.1}.
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DR   EMBL; AAPJ01000001; EAS51630.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1YLV1; -.
DR   HOGENOM; CLU_054952_0_0_5; -.
DR   BioCyc; AURANTIMONAS:SI859A1_02446-MONOMER; -.
DR   Proteomes; UP000000321; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 2.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:EAS51630.1};
KW   Hydrolase {ECO:0000313|EMBL:EAS51630.1};
KW   Protease {ECO:0000313|EMBL:EAS51630.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000321}.
SQ   SEQUENCE   409 AA;  44159 MW;  D28250F01331F673 CRC64;
     MGTRRHAEHA GAAMWFRLLA TVFAVLLLQA PAFADVKDRI ASLAPSGLVF VLDEDGNELL
     AQNADQPFVP ASVAKLVTAW LAMEELGGDY RFKTQFYLGD DRVLYVRGGG DPFLVSEELA
     VLAPKLLDET GTEPFTGIVV DASYYPAELR IPGIEATDEA YDALNSALAV NFNTINARRN
     GKTVRSAEEQ TPITPLAISQ FRARGPNGRS RISLTQEDPS IGIRYAGELL AAFIERSGGS
     VKGEISLGPV AAGLTPVYVH EQSRDLAEIL RQMLIGSNNY IANQVFLEIG AQREGGPVSL
     GKSIRVAREI FAAHDVPDAM QLVEGSGISR DNSFTARGLA RVLGHFAPHA ELLRKTRAGS
     RYKTGTFSGV STLAGFARTA EHGDVRFVIS LNGGGKLRFR LLTAIERDF
//