ID R7MLL4_9FIRM Unreviewed; 365 AA.
AC R7MLL4;
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=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:CDF01969.1};
GN ORFNames=BN739_01506 {ECO:0000313|EMBL:CDF01969.1};
OS Ruminococcus sp. CAG:624.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262965 {ECO:0000313|EMBL:CDF01969.1, ECO:0000313|Proteomes:UP000017977};
RN [1] {ECO:0000313|EMBL:CDF01969.1, ECO:0000313|Proteomes:UP000017977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:624 {ECO:0000313|Proteomes:UP000017977};
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:CDF01969.1}.
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DR EMBL; CBKC010000292; CDF01969.1; -; Genomic_DNA.
DR AlphaFoldDB; R7MLL4; -.
DR STRING; 1262965.BN739_01506; -.
DR MEROPS; M15.024; -.
DR Proteomes; UP000017977; 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; 2.60.40.1080; -; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
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; PF02368; Big_2; 1.
DR Pfam; PF02557; VanY; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:CDF01969.1};
KW Hydrolase {ECO:0000313|EMBL:CDF01969.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CDF01969.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017977};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..174
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
SQ SEQUENCE 365 AA; 39711 MW; 182BFCC17E21B99A CRC64;
MSQKRVTQQT LRRRRLVAML ILLFIIIMGF VLISKSCSSS DKDKKGNTKV KSSTTTAVTA
TTMPTQQSAV TNTTTVRPEG TGTEIVTATA TGTPDGSTVE SITLTFYSAN LQIGESKMPI
VTMNPATAAN KSERWETSNK SIATVDELGN ITGVSAGTCY ITVYSVSSPE VYAEVKVKVV
EGDDVQPQSN ASASQPTYVD GILIANKSYS LPEDYNPGLD TTTKSQFDSL SAAAAKEGLN
IYLSSGFRSY SDQSAIYNNY VNNYGQATAD TFSARPGYSE HQTGLAIDVN TIDDSFAGTP
EAVWLENHAH EYGFIIRYPK GKESITGYKY EPWHIRYLGV EKATDVYNSG KTLEEYLNID
SKYSN
//
