ID H3NJR1_9LACT Unreviewed; 343 AA.
AC H3NJR1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=LD-carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9708_01100 {ECO:0000313|EMBL:EHR36874.1};
OS Facklamia languida CCUG 37842.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=883113 {ECO:0000313|EMBL:EHR36874.1, ECO:0000313|Proteomes:UP000006190};
RN [1] {ECO:0000313|EMBL:EHR36874.1, ECO:0000313|Proteomes:UP000006190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 37842 {ECO:0000313|EMBL:EHR36874.1,
RC ECO:0000313|Proteomes:UP000006190};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Facklamia languida CCUG 37842.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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:EHR36874.1}.
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DR EMBL; AGEG01000013; EHR36874.1; -; Genomic_DNA.
DR RefSeq; WP_006309282.1; NZ_JH601133.1.
DR AlphaFoldDB; H3NJR1; -.
DR STRING; 883113.HMPREF9708_01100; -.
DR PATRIC; fig|883113.3.peg.1093; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_1_0_9; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000006190; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd07062; Peptidase_S66_mccF_like; 1.
DR Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237:SF4; CARBOXYPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000006190}.
FT DOMAIN 6..129
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 203..330
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
SQ SEQUENCE 343 AA; 38595 MW; 111BBDEB9336BF57 CRC64;
MKIKKIGIVS LSSGLLGEAF VDHQIAIGLE RLISLGLEVE FLPNSRKGIT YLQAHPEARA
EDLLQAMADD SIDMILCAIG GDDTYRLAPH LFDQDALAKV AKQKVFLGFS DTTANHFMFH
KLGIKTFYGQ AFLPDIAELS DQMLDYTAHY FEELIHKGRI TEIRPSDVWY PNREDFGVSQ
VGTEMPAYQN NGFELLQGPT KFEGEILGGC LESIDQFFNN ARHADSVAIT NKYQLFPSLE
DWRDKILLLE TSEEKTAPDL FKKMIQTLAD YGIFEVLSGL LVGKPQDEAY YEAYKDILVQ
EIGNTNLPIL YNLNVGHAMP RCIVPFGVPA FVDAVEQRIR FED
//
