ID A0A1C3EFZ4_9GAMM Unreviewed; 333 AA.
AC A0A1C3EFZ4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Peptidase S66 {ECO:0000313|EMBL:ODA32158.1};
GN ORFNames=A8L45_13935 {ECO:0000313|EMBL:ODA32158.1};
OS Veronia pacifica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Veronia.
OX NCBI_TaxID=1080227 {ECO:0000313|EMBL:ODA32158.1, ECO:0000313|Proteomes:UP000094936};
RN [1] {ECO:0000313|EMBL:ODA32158.1, ECO:0000313|Proteomes:UP000094936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 1920 {ECO:0000313|EMBL:ODA32158.1,
RC ECO:0000313|Proteomes:UP000094936};
RA Gomez-Gil B., Enciso-Ibarra J.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (MAY-2016) 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:ODA32158.1}.
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DR EMBL; LYBM01000026; ODA32158.1; -; Genomic_DNA.
DR RefSeq; WP_068903297.1; NZ_LYBM01000026.1.
DR AlphaFoldDB; A0A1C3EFZ4; -.
DR STRING; 1080227.A8L45_13935; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000094936; 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:SF5; CARBOXYPEPTIDASE YOCD-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:UP000094936}.
FT DOMAIN 15..134
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 205..320
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 305
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 333 AA; 36917 MW; F3CAD9110F24A29F CRC64;
MEKTLPPALK KGDTIAFFSP STPITALATG RFERARHFLS EKGFILKAGS LTGKTDHYRS
GSIQERAEEL NALIRDPAVR CIMSTIGGMN SNALLPYIDY EALLKDPKII IGYSDVTALL
SGIYAKTGLI TFYGPALVAS FGEFPPMVDD TYDSFKQLVI NGMGQSHQYT MPEAWTDEFI
DWKTQSGPKS TQPNQWVFQG QGVYTGRLIG GNLNTMAGIW GSPYMPEIED GDILLLEDSL
KGIESVERSF AHLKACGVFD RVSAVLLGKH EKFNDKGTKR QPIDVLREVL NDQPLPIVVD
FDCCHTHPML TMPLGATVTV DFEQETVRLE DKW
//
