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Database: UniProt
Entry: A0A292RHN6_9BACT
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ID   A0A292RHN6_9BACT        Unreviewed;       447 AA.
AC   A0A292RHN6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:DAA97817.1};
GN   Name=dacB {ECO:0000313|EMBL:DAA97817.1};
GN   ORFNames=CPT80_01370 {ECO:0000313|EMBL:DAA97817.1};
OS   Candidatus Gastranaerophilales bacterium HUM_9.
OC   Bacteria; Candidatus Melainabacteria; Candidatus Gastranaerophilales.
OX   NCBI_TaxID=1916320 {ECO:0000313|EMBL:DAA97817.1, ECO:0000313|Proteomes:UP000218540};
RN   [1] {ECO:0000313|EMBL:DAA97817.1, ECO:0000313|Proteomes:UP000218540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HUM_9 {ECO:0000313|EMBL:DAA97817.1};
RX   PubMed=28360330; DOI=.1126/science.aal3794;
RA   Soo R.M., Hemp J., Parks D.H., Fischer W.W., Hugenholtz P.;
RT   "On the origins of oxygenic photosynthesis and aerobic respiration in
RT   Cyanobacteria.";
RL   Science 355:1436-1440(2017).
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:DAA97817.1}.
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DR   EMBL; DABG01000004; DAA97817.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A292RHN6; -.
DR   STRING; 1916320.GCA_002103075_00666; -.
DR   Proteomes; UP000218540; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.710.10; 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:DAA97817.1};
KW   Hydrolase {ECO:0000313|EMBL:DAA97817.1};
KW   Protease {ECO:0000313|EMBL:DAA97817.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..447
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012697012"
SQ   SEQUENCE   447 AA;  50354 MW;  DACC24A975DEFFE0 CRC64;
     MKKFLTLFIL LMFGFNTNVF ANDIKQAVNT AISNSSVSKG SISVSIKDVN TGKTVYELNP
     KMPTPPASIQ KIVTSTPAFI LLGDDYKFQT KLYKNNKDEY LLVLGADPYL RTKDLTKIVK
     ALPKEIKLLA IDDSIIDDKE WGEGWQWDDD LNPLMPKFSA YNIDKNLMEV AVVPTVKGCS
     ADIRTTVNYP TTFVNHIITD TKTDYKMTRQ NYVSPDIITI EGTVEQKKSI IKQIPINSPK
     KYFKLRLSDA IIDANLSCSG VYPRKRLTSD YRLITYLSHD GINAQSDILK RSNNLMAETV
     FKIAGKKYMG KNGTGSFEDG LKMLSDFCKK QNIDTSNINI VDASGVSKNN IMTADFMTEF
     LLKNCNYLEH RLTTAGEGTL SDRMFYLKDK LYAKTGTLSN ISSITGYITT KKNNKYVFCI
     MINTAKLKEA DKKMLEEYIL RGIYIAG
//
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