ID G1WC11_9BACT Unreviewed; 415 AA.
AC G1WC11;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9431_01362 {ECO:0000313|EMBL:EGV31194.1};
OS Segatella oulorum F0390.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=702438 {ECO:0000313|EMBL:EGV31194.1, ECO:0000313|Proteomes:UP000005141};
RN [1] {ECO:0000313|EMBL:EGV31194.1, ECO:0000313|Proteomes:UP000005141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0390 {ECO:0000313|EMBL:EGV31194.1,
RC ECO:0000313|Proteomes:UP000005141};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella oulorum F0390.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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:EGV31194.1}.
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DR EMBL; ADGI01000046; EGV31194.1; -; Genomic_DNA.
DR RefSeq; WP_004380402.1; NZ_JH114216.1.
DR AlphaFoldDB; G1WC11; -.
DR PATRIC; fig|702438.4.peg.1406; -.
DR eggNOG; COG2027; Bacteria.
DR HOGENOM; CLU_017692_1_3_10; -.
DR Proteomes; UP000005141; 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 PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005141};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..415
FT /note="D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-
FT alanine-endopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003425939"
SQ SEQUENCE 415 AA; 45881 MW; 94E414CEC6DBCDC6 CRC64;
MMKLKIIVPA LLGAMALTLT CGACGGGKSN DKQNKPAAVP KDIAVDQQLR TRLEAFAEDM
KLRGVFGFQV YDITANKPVY GYHEHRTQPS ASCLKLLTGV AGLHFLGTHY NYRTAIFIKG
RQVGDTLQGD VSFKADLDPM LQPDDLDMFV QALRRKGIQN IAGKLIFDLV LTDPVTSEAH
WYPWDLSFSH YGLLYKGEAK VKQALQQSLR HAGIMVSDEQ MVVAKTPAGS HCLFRFYRSI
DRVIQRMWKN SSNTQATSLL YTIGHYYDPK QAPAEAGLAY LRHFMRKNLQ LKDSALVIHD
GCGLCTHNQL SPDALVIILR YGYAHPAIYG QLQRNLSIAG VDGTLHSLLQ SDKLKGKIHG
KTGTLSHPYG ISSLAGYATG SNGHLLAFAI MDHQMSVLDA RVLQRELCTV LVDKP
//
