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Database: UniProt
Entry: R7GUY2_9FIRM
LinkDB: R7GUY2_9FIRM
Original site: R7GUY2_9FIRM 
ID   R7GUY2_9FIRM            Unreviewed;       384 AA.
AC   R7GUY2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:CDE29717.1};
GN   ORFNames=BN645_00867 {ECO:0000313|EMBL:CDE29717.1};
OS   Ruminococcus sp. CAG:403.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262958 {ECO:0000313|EMBL:CDE29717.1, ECO:0000313|Proteomes:UP000017925};
RN   [1] {ECO:0000313|EMBL:CDE29717.1, ECO:0000313|Proteomes:UP000017925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:403 {ECO:0000313|Proteomes:UP000017925};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDE29717.1}.
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DR   EMBL; CBIS010000004; CDE29717.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7GUY2; -.
DR   STRING; 1262958.BN645_00867; -.
DR   Proteomes; UP000017925; 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   Gene3D; 3.30.200.180; -; 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:CDE29717.1};
KW   Hydrolase {ECO:0000313|EMBL:CDE29717.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CDE29717.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017925};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          136..262
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
FT   REGION          348..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  42262 MW;  D45134F1EA4B037A CRC64;
     MANKQTMNQK QAEKAKGQKP EHSVRAGLVA LDLFLSLAVV GTVGFYLYRV GSSFEKIDML
     ESSTLLAASG EESSQPEAEG DQSVYDNVFV KTDAVYSGDL ILVNNDTEYH SGQETDLVNL
     YEKKTDHYHL SGTEMMLREE AVSGFNALMD AFYVASGRDD IIVISGYRTK EEQQGLYDED
     LQQTGADSSS RVSLPGHSEH ESGYAVDLSL FTDGVLADYD GTGDYAWINE NCAKYGFVLR
     YTEQKQPITG IEPEPWHYRY VGQPHATYMT EHDLCLEEYL DSLRQYSAEN PLTIENWDGE
     LYQVYFVPAD MSADGTYALI PTNASYTISG NNKDGYIVTV DTGEIQSFDS AADSSTDSAA
     ESESTAEAES EPADASDSEV SASE
//
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