ID   A0A1M6F9K8_9CLOT        Unreviewed;       281 AA.
AC   A0A1M6F9K8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=D-Ala-D-Ala carboxypeptidase. Metallo peptidase. MEROPS family M15B {ECO:0000313|EMBL:SHI94360.1};
GN   ORFNames=SAMN05444401_1855 {ECO:0000313|EMBL:SHI94360.1};
OS   Clostridium amylolyticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121298 {ECO:0000313|EMBL:SHI94360.1, ECO:0000313|Proteomes:UP000184080};
RN   [1] {ECO:0000313|EMBL:SHI94360.1, ECO:0000313|Proteomes:UP000184080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21864 {ECO:0000313|EMBL:SHI94360.1,
RC   ECO:0000313|Proteomes:UP000184080};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQZO01000002; SHI94360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6F9K8; -.
DR   STRING; 1121298.SAMN05444401_1855; -.
DR   Proteomes; UP000184080; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd14852; LD-carboxypeptidase; 1.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR003709; Pept_M15B.
DR   PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR   Pfam; PF02557; VanY; 1.
DR   SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:SHI94360.1};
KW   Hydrolase {ECO:0000313|EMBL:SHI94360.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SHI94360.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184080};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        5..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          132..259
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
FT   REGION          40..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  32020 MW;  3F76695B05E725FE CRC64;
     MKKYIGLFTV FIAVAVVFIF IMINKSNGVV TNARFMGRQA SANSEKYQDD NETENNIIDD
     KNIKDNSVEN RDGTSTTKES QNNNQETNKQ NNKSASDILL ANKSHRLDKD YVPKNLTLPK
     VKFKSSVDDL VKKMDKEAAL ALEDMFNAAK QDGITLLGVS GYRSYAIQNN LYNSNVKRQG
     KSHADRYSAQ PGASEHQTGL AMDMLSTDYS SLNEGFENTK AFKWLEDNAY KYGYILRYPK
     GKENITGYAY EPWHYRYVGI EVSEKITKNK LTLEEYLREN N
//