ID   A0A1H5KZT3_9ACTN        Unreviewed;       410 AA.
AC   A0A1H5KZT3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:SEE69458.1};
GN   ORFNames=SAMN05216533_3286 {ECO:0000313|EMBL:SEE69458.1};
OS   Streptomyces sp. Ag109_O5-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEE69458.1, ECO:0000313|Proteomes:UP000198812};
RN   [1] {ECO:0000313|EMBL:SEE69458.1, ECO:0000313|Proteomes:UP000198812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEE69458.1,
RC   ECO:0000313|Proteomes:UP000198812};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNTQ01000001; SEE69458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5KZT3; -.
DR   STRING; 1855349.SAMN05216533_3286; -.
DR   Proteomes; UP000198812; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
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   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:SEE69458.1};
KW   Hydrolase {ECO:0000313|EMBL:SEE69458.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SEE69458.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198812};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..410
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011731418"
FT   TRANSMEM        373..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..301
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   REGION          336..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  42369 MW;  BF442DC69BEAE764 CRC64;
     MLLVASAALL SLSSTAPAAL AAPTPSTTPS ATPPAGMSTV GGARLGQPGT QVNLAAGVPV
     LPKDVTARSW IVSDAESGEV LAAHNAHWRL PPASTLKMLF ADTVLPRFPK TTPHKVVPAD
     LAGIGAGSSM VGIKEGQTYT VHDLWLGVFL RSGNDAVHVL SAMNGGVEQT VKDMQDHADE
     LQALDTHVVS PDGYDQPGQV SSAYDLSLFA RSGLQKKDFR EYCSTVRASF PGDTTKNAKG
     KPVRGSFEIQ NTNRLLSGDT DVPVYQGIAG VKNGNTTNAG ATFTGVAERN GRVLLVTVMN
     PEKKEHNEVY KETAKLFDWG FQAAGKVTPV GELVPPKGAA TSSASPRATA AGKDDGASAK
     PVAAASANGS GGVGVALGIA GGVVVLLAGA AFVVNRRWPL PDLVRRRTRP
//