ID A0A0G9H762_9GAMM Unreviewed; 323 AA.
AC A0A0G9H762;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase S66 {ECO:0000313|EMBL:KLD65094.1};
GN ORFNames=Y882_04465 {ECO:0000313|EMBL:KLD65094.1};
OS Dyella japonica DSM 16301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1440762 {ECO:0000313|EMBL:KLD65094.1, ECO:0000313|Proteomes:UP000035481};
RN [1] {ECO:0000313|EMBL:KLD65094.1, ECO:0000313|Proteomes:UP000035481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16301 {ECO:0000313|EMBL:KLD65094.1,
RC ECO:0000313|Proteomes:UP000035481};
RX PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT "A phylogenomic and molecular marker based taxonomic framework for the
RT order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT containing the genus Rhodanobacter and its closest relatives.";
RL Antonie Van Leeuwenhoek 107:467-485(2015).
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:KLD65094.1}.
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DR EMBL; JPLA01000011; KLD65094.1; -; Genomic_DNA.
DR RefSeq; WP_046970676.1; NZ_JPLA01000011.1.
DR AlphaFoldDB; A0A0G9H762; -.
DR STRING; 1440762.Y882_04465; -.
DR PATRIC; fig|1440762.4.peg.220; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000035481; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07025; Peptidase_S66; 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; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30237:SF2; MUREIN TETRAPEPTIDE 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 Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 6..128
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 172..288
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT REGION 304..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 323 AA; 34943 MW; 41B04AA535012056 CRC64;
MTSPSIRLIA PSGYPHDRDA MARGIARLQA AGCTVDGVDV LDRVEHRFAG PDAVRAADIN
ALATMQQLPD IALSIRGGYG ATRLLEHLHY DALRERLAGS NTLLVGHSDF TAVQMALYAK
TGLVTFGGPM LGPDFGAPEL NGLMWEHFWR AVGEAQATAS WSTTSTTGLD VEGPLWGGNL
AMLCSLLGTP YFPHIDDGIL FVEDIGEPPF RLERLLYQLR LAGVLDRQRA LVLGHFTQCR
PHAYDNGYDT EAAFEQLARV ARIPIIRNLP FGHEPDKFTL PFGVPARLKV AAGQASLSFR
GHPTLAGAVS RPDPGTPPLH PVK
//
