ID A0A197SPN2_9ACTN Unreviewed; 440 AA.
AC A0A197SPN2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=A8W25_21155 {ECO:0000313|EMBL:OAR24848.1};
OS Streptomyces sp. ERV7.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1322334 {ECO:0000313|EMBL:OAR24848.1, ECO:0000313|Proteomes:UP000078470};
RN [1] {ECO:0000313|EMBL:OAR24848.1, ECO:0000313|Proteomes:UP000078470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERV7 {ECO:0000313|EMBL:OAR24848.1,
RC ECO:0000313|Proteomes:UP000078470};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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:OAR24848.1}.
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DR EMBL; LYOY01000040; OAR24848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197SPN2; -.
DR STRING; 1322334.A8W25_21155; -.
DR Proteomes; UP000078470; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF33; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB1; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000078470};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..440
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008277271"
FT DOMAIN 81..312
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 26..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 440 AA; 44051 MW; BA057C8D35493AD6 CRC64;
MQFSRPLAIA ALTAAAVVSA VAPAAAHPVK PGTPSPGKPT PGVPRAGAPK EPPAAMSTLG
GEQLGRPGPQ TGVGAPALPA GLSSLAWMVS DADTGQVLAA SNAHWPLPPA STLKMLFADT
VLPVVPGTVS HKVEPAELAG MGDGSSAVGI VPGQTYLGAD LWRGVFLRSG NDAVHVLAAM
NGGVPKTVTD MQAKAESLGA KDTHVRSPDG YDAEGQVSSA YDLTLFLRSG LRNKDFKEYC
ATADAKFPGG PNTKGKPFGI SNTNRMLSGI GGVSKYPGLI GGKNGYTTHA GNTLAEAATR
DGHTILVTVM NPQENKHDKV YTETRALLDW GFAAVGRAKP VGTLDPAKPT PPAKPKGTAS
ATTDSSGLGV LGWTGLGAGA AVAAGGGVCG AEAAAGEAAA GVRDRTSSGP HLMGCGPRPD
CGSRMGPCTA ACYSGLPSVM
//
