ID A0A0W0Z7M2_9GAMM Unreviewed; 597 AA.
AC A0A0W0Z7M2;
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 {ECO:0000313|EMBL:KTD65129.1};
GN Name=dacB {ECO:0000313|EMBL:KTD65129.1};
GN ORFNames=Lsha_0498 {ECO:0000313|EMBL:KTD65129.1};
OS Legionella shakespearei DSM 23087.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD65129.1, ECO:0000313|Proteomes:UP000054600};
RN [1] {ECO:0000313|EMBL:KTD65129.1, ECO:0000313|Proteomes:UP000054600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD65129.1,
RC ECO:0000313|Proteomes:UP000054600};
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:KTD65129.1}.
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DR EMBL; LNYW01000016; KTD65129.1; -; Genomic_DNA.
DR RefSeq; WP_018578512.1; NZ_LNYW01000016.1.
DR AlphaFoldDB; A0A0W0Z7M2; -.
DR STRING; 1122169.Lsha_0498; -.
DR PATRIC; fig|1122169.6.peg.570; -.
DR eggNOG; COG2027; Bacteria.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000054600; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
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:KTD65129.1};
KW Hydrolase {ECO:0000313|EMBL:KTD65129.1};
KW Protease {ECO:0000313|EMBL:KTD65129.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..597
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006918380"
SQ SEQUENCE 597 AA; 65021 MW; E85E2D813EF4E9F4 CRC64;
MKKTLIGVCL WSLWSIPASY ASLQSGVDKL INRLNPNVNL GMVVFDLNSG ETLYKRNADH
LFIPASNMKL FSEAATLMAL GPDYRFKNQL STSASQLQQG VLHGNLYLHL SGDPSFTRHD
LNQLLSKLKD WNITAIEGNI FIDSSLTSIP AYPPGWLAAD LAYSYGAPIA PLMVDANRLT
VTVNPGAKVG DPAIVEVDDG GGTINLTNQA QTKATEKGCG VGFTLDPENN LTVRGCVGLG
QWAVQQRLAI KHPLVYIDGM IKSQLAKANI QFNGKIDLGR APAGSLLIAT EYSKPVSQLM
ADTLKPSDNL YADSLYLHAA AKINGSPVNW NQAEPVVKKF LQQQTGIDFS KATFTDGSGL
SRYNLVTPEQ TLALLKFLYQ RFSLAYEYIA ALPISGRDGT LQKRFKTPGQ QGFIRAKTGT
MTGMNSLSGY LYTANGHTLA FAMYINKQPG KSSGPGRPLL DALCTYFLAQ SPGNGSLARV
FAPHNRVKFQ SNPTQGEVQR NHQAKWRRLE SQVKFALKGQ DVTVIYRGNE LIVTDNQSDA
NKVWSALQSV GKKYPFAVAL SSPSLTVSPQ GKPMVLWVQT PSTAEGAQRT WTIREAV
//
