ID   A0A0W0ZZ07_9GAMM        Unreviewed;       595 AA.
AC   A0A0W0ZZ07;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:KTD74335.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:KTD74335.1};
GN   ORFNames=Ltuc_2182 {ECO:0000313|EMBL:KTD74335.1};
OS   Legionella tucsonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=40335 {ECO:0000313|EMBL:KTD74335.1, ECO:0000313|Proteomes:UP000054693};
RN   [1] {ECO:0000313|EMBL:KTD74335.1, ECO:0000313|Proteomes:UP000054693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49180 {ECO:0000313|EMBL:KTD74335.1,
RC   ECO:0000313|Proteomes:UP000054693};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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:KTD74335.1}.
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DR   EMBL; LNZA01000001; KTD74335.1; -; Genomic_DNA.
DR   RefSeq; WP_058521300.1; NZ_LNZA01000001.1.
DR   AlphaFoldDB; A0A0W0ZZ07; -.
DR   STRING; 40335.Ltuc_2182; -.
DR   PATRIC; fig|40335.7.peg.2323; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000054693; Unassembled WGS sequence.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   NCBIfam; TIGR00666; PBP4; 1.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 1.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KTD74335.1};
KW   Hydrolase {ECO:0000313|EMBL:KTD74335.1};
KW   Protease {ECO:0000313|EMBL:KTD74335.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054693}.
SQ   SEQUENCE   595 AA;  65199 MW;  D8A8E240A17E5363 CRC64;
     MKRTFTGAFL LALSTLSYGI SIQGEVDKLI SRINPKVNLG VVVLDLTSGQ TLYRRNAGRL
     YIPASNMKLF SEAAALMILG PDYRFENRLS MSAGTIQQGI LQGNVYVQLS GDPSFNRNDL
     KALLSSLKEW NINTIQGNVY IDSSLAQVDP YPPGWLATDL SYSYGAPNAP VMVDSNRLTV
     TVNPGAQAGD PAIVEVDDGG GAIALNNQAT TKPNAKGCGV GFNLDQDNHL TVRGCVGVGQ
     WAVQQRLAIK NPLMYAQSMI KTQLKKDNIQ LNGQVQLGET PEGSLLIATQ HSKPVSQLMA
     DTLKPSDNLY ADSLYLHAAK QLTGASVNWR DAEPLIKNFL QSQTGIDFTN AIFTDGSGLS
     RYSLVTPEQT ISLLKFLYQR FPLSYEYISA LPISGRDGTL QKRFRIPTQQ GFVRAKTGTM
     TGINSLSGYL YTANGHTLAF AMYVNRQPGK TSGPGRPVLD ALCTYFLQKN PDSNSLSRIF
     SPHQRISFQS NPTQADKQKA HQAKWRRLES AIRTALRGQP VNIIYRGNEL IVTDNQADPE
     KVWTALQSVV KKYPFGVMLS SKILSINPSG SPSLLWVQAD TPNQVQRTWS IREAA
//