ID   A0A0G0TXK0_9BACT        Unreviewed;       307 AA.
AC   A0A0G0TXK0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase family protein {ECO:0000313|EMBL:KKR51845.1};
GN   ORFNames=UT89_C0005G0002 {ECO:0000313|EMBL:KKR51845.1};
OS   Parcubacteria group bacterium GW2011_GWE1_40_20.
OC   Bacteria.
OX   NCBI_TaxID=1618946 {ECO:0000313|EMBL:KKR51845.1, ECO:0000313|Proteomes:UP000034131};
RN   [1] {ECO:0000313|EMBL:KKR51845.1, ECO:0000313|Proteomes:UP000034131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKR51845.1}.
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DR   EMBL; LBYN01000005; KKR51845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0TXK0; -.
DR   Proteomes; UP000034131; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:KKR51845.1};
KW   Hydrolase {ECO:0000313|EMBL:KKR51845.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KKR51845.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          154..276
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
SQ   SEQUENCE   307 AA;  35310 MW;  323E9701FAA2E2BA CRC64;
     MNNKEHEHHI ALKSPLTYSV MVVFVILILF IAFGTYQYYI QNVVLKQTKL ELVTKEEISE
     QNIRLLREAL LSKNNENAVL YNSLTQEQTR NNLFGEQIQT LSSTVGLLDK LSKTDRELLQ
     KYSNIYFLNE NYTPSSLAEI DPTFLYRDSK PETIHGSIKP YLENMLRSAN ANAKPLLVLS
     AYRSFGTQAS IKTGYKVTYG TTAANKFSAD QGYSEHQLGS TVDLTTLAGG ETLTGFDKTE
     SFKWLTENAY AYGFILSYPK GNKFYQFEPW HWRFVGVELA TKLHNENKNF YDVDQREINE
     YLVKIFD
//