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Database: UniProt
Entry: A0A1A3QQF3_9MYCO
LinkDB: A0A1A3QQF3_9MYCO
Original site: A0A1A3QQF3_9MYCO 
ID   A0A1A3QQF3_9MYCO        Unreviewed;       415 AA.
AC   A0A1A3QQF3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:OBK48315.1};
GN   ORFNames=A5655_04660 {ECO:0000313|EMBL:OBK48315.1};
OS   Mycobacterium sp. 1081908.1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834066 {ECO:0000313|EMBL:OBK48315.1, ECO:0000313|Proteomes:UP000092324};
RN   [1] {ECO:0000313|Proteomes:UP000092324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1081908.1 {ECO:0000313|Proteomes:UP000092324};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA   Lopez-Varela E., Palencia S.;
RL   Submitted (JUN-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:OBK48315.1}.
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DR   EMBL; LZLY01000088; OBK48315.1; -; Genomic_DNA.
DR   RefSeq; WP_067010455.1; NZ_LZLY01000088.1.
DR   AlphaFoldDB; A0A1A3QQF3; -.
DR   STRING; 1834066.A5655_04660; -.
DR   OrthoDB; 3663940at2; -.
DR   Proteomes; UP000092324; 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: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   Carboxypeptidase {ECO:0000313|EMBL:OBK48315.1};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Protease {ECO:0000313|EMBL:OBK48315.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..415
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038660689"
FT   TRANSMEM        384..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          97..318
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   REGION          42..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        132
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   415 AA;  42417 MW;  61A9B5F75842BB75 CRC64;
     MSLLRSASCL AATAFMVGVM VAAPIAVPVA LAEPAPGPAA GPPNCPFQVN TPPAVDSSEV
     PAAGDPPIPL AVPPKPVGGE ALGGCGVVAA PGTPPLPGDV SADAWLVADL DSGAVIAAKD
     PHGRHRPASI IKVLVAMASI NALPLNKSVE GTADDAAAEG TKVGVTDGGV FTVNQLLHGL
     LMHSGNDAAH ALAVQLGGMQ QALDKINVLA AKLGGRDTRV ATPSGLDGPG MSTSAYDIGL
     FYRYAWQNPT FAGIVATRTF DFPGHGDHPG YELENDNQLL YKYPGAMGGK TGYTDDAGQT
     FVGAANHDGR RLMAVLLHGT RQPIAPWEQA AHLLDYGFST PQGTQVGTLI EPDPSLMPAK
     RDSAADRPGA GPQAAGLLPS ADALPVRVGV AVIGTIIVFS LIMVARSMNR RPQHR
//
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