ID A0A426VFW1_9BURK Unreviewed; 373 AA.
AC A0A426VFW1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:RRS05826.1};
GN ORFNames=EIP75_02885 {ECO:0000313|EMBL:RRS05826.1};
OS Aquabacterium soli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Aquabacterium.
OX NCBI_TaxID=2493092 {ECO:0000313|EMBL:RRS05826.1, ECO:0000313|Proteomes:UP000269265};
RN [1] {ECO:0000313|EMBL:RRS05826.1, ECO:0000313|Proteomes:UP000269265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJQ9 {ECO:0000313|EMBL:RRS05826.1,
RC ECO:0000313|Proteomes:UP000269265};
RA Sun L., Gao X., Chen W., Huang K.;
RT "The whole draft genome of Aquabacterium sp. SJQ9.";
RL Submitted (DEC-2018) 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:RRS05826.1}.
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DR EMBL; RSED01000002; RRS05826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A426VFW1; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000269265; 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 ECO:0000313|EMBL:RRS05826.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000269265};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 69..178
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 247..362
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 277
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 373 AA; 40060 MW; 3B984D10E4D8906C CRC64;
MSARPAAKKS ASRKNAAAAA HDHGDHGHAH AHAHAHAHAH AHEHHDHGCG PDCGHDHGDM
LQRPRRLTVF SPAGVVAKAA QGRRAVKRLK ALGFDASLDT DALSKHQRFA GEDDVRLAAL
HRVAEDAPDV ALAARGGYGL MRLLDRIDWP LIARSIERGT AWVGYSDVTA FQLAALAHNA
AGPASAPHGI TAGLWAGPMA CGDFGSDDNP DGGDDVTQEC FVEAMTGQLE AVGFRTEAGF
DGLETAGRLW GGNLSILQAL LGTPHFPKIK NGVLFLEDVN EHPYRIERAL LQLHQAGVLD
QQKAIVLGAF TEYRKSPLDR GYTIKSTIEH LRSVTRTPIL TGLPFGHVPT KLSLPLGRKV
NVVVQGRDVF VMW
//
