ID   E6MFF7_9FIRM            Unreviewed;       237 AA.
AC   E6MFF7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:EFV02144.1};
GN   ORFNames=HMP0721_0740 {ECO:0000313|EMBL:EFV02144.1};
OS   Pseudoramibacter alactolyticus ATCC 23263.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Pseudoramibacter.
OX   NCBI_TaxID=887929 {ECO:0000313|EMBL:EFV02144.1, ECO:0000313|Proteomes:UP000004754};
RN   [1] {ECO:0000313|EMBL:EFV02144.1, ECO:0000313|Proteomes:UP000004754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23263 {ECO:0000313|EMBL:EFV02144.1,
RC   ECO:0000313|Proteomes:UP000004754};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:EFV02144.1}.
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DR   EMBL; AEQN01000012; EFV02144.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6MFF7; -.
DR   STRING; 887929.HMP0721_0740; -.
DR   eggNOG; COG1876; Bacteria.
DR   HOGENOM; CLU_054193_1_2_9; -.
DR   Proteomes; UP000004754; Unassembled WGS sequence.
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:EFV02144.1};
KW   Hydrolase {ECO:0000313|EMBL:EFV02144.1};
KW   Protease {ECO:0000313|EMBL:EFV02144.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004754}.
FT   DOMAIN          79..207
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   237 AA;  26100 MW;  290025245083F1CF CRC64;
     MTSVRACTRR KRHAAQKQQT KTEAQSPKQP ALSPQTKLKN AAAQTGNTAQ LINKTHTLPP
     SYVPKDLVKV NAASYRTVYL RKEAAQALAT MFNAGKKAGV NLYCSSGYRS YADQQKIFSN
     HMASMGRARA NAISSKAGQS EHQSGFAMDV TCRAMSGDLQ ERFIQTNEGK WLAAHAHEYG
     FIVRFPKGKE ASTGYSYEPW HIRYLGKDLA TKVNASGLSY EEYLAKNAKL ATVIDGQ
//