ID R6YZV2_9FIRM Unreviewed; 560 AA.
AC R6YZV2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:CDD34151.1};
GN ORFNames=BN600_00509 {ECO:0000313|EMBL:CDD34151.1};
OS Roseburia sp. CAG:309.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1262945 {ECO:0000313|EMBL:CDD34151.1, ECO:0000313|Proteomes:UP000018292};
RN [1] {ECO:0000313|EMBL:CDD34151.1, ECO:0000313|Proteomes:UP000018292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:309 {ECO:0000313|Proteomes:UP000018292};
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 -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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:CDD34151.1}.
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DR EMBL; CBGX010000010; CDD34151.1; -; Genomic_DNA.
DR AlphaFoldDB; R6YZV2; -.
DR STRING; 1262945.BN600_00509; -.
DR Proteomes; UP000018292; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF119; OS02G0119300 PROTEIN; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CDD34151.1};
KW Hydrolase {ECO:0000313|EMBL:CDD34151.1};
KW Protease {ECO:0000313|EMBL:CDD34151.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018292};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..560
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004426094"
FT DOMAIN 274..549
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 560 AA; 62790 MW; 208322B29756E5AC CRC64;
MASHKNKKQL VWLLLTALFF TQMPANEAKA QTTLPSGTPY PIASASPLPT TTTTVEPIVS
TNTPFGIYPT ASATTIPSAV PTASPKATPF TLLNKNAVRQ VSKKKVQYRI NSYVTDTVVL
KTSVKAKFEP VGETISLCRR GILKIEKNGQ VKCTKKGQSK AQNCQIKVTE ATGERSFTVK
IRFEKKLENK GKGAELIYQG KQAQIRTNYK MNRLTFTSSN KKAASVDKKG KITARKKGKT
TISVKVKGSE KNEFKIRITV KEEPWIVNVK DSRYTYEDMT SDLRKIAWKY RGKAALQNLG
SSEDGRAIWC LRIGSPYASK KYLINGGIHA REWLNCQMLT HKSEEILREY ADYKSALKGK
CIYIIPMINP DGVTISQFGF DAIRNPKLRK ICKKTKNSAR TWKGNARGVN LNFNCPGGWN
KKGKSKKADG LSYPGKKAAS EKETRVMMNF VNRISGWKAS LNYHSTGSIL YWNYNVESEA
SLYERQKALA EKVNSFTHYR LMPKSISTDP NGGFGDWLIY NKKIPNVTVE TGSVMSPLPH
SQLKKIQKEN GELLSWFIKQ
//