ID R9GXJ9_9SPHI Unreviewed; 298 AA.
AC R9GXJ9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:EOR96542.1};
DE EC=3.4.17.13 {ECO:0000313|EMBL:EOR96542.1};
GN ORFNames=ADIARSV_0271 {ECO:0000313|EMBL:EOR96542.1};
OS Arcticibacter svalbardensis MN12-7.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Arcticibacter.
OX NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR96542.1, ECO:0000313|Proteomes:UP000014174};
RN [1] {ECO:0000313|EMBL:EOR96542.1, ECO:0000313|Proteomes:UP000014174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN12-7 {ECO:0000313|EMBL:EOR96542.1,
RC ECO:0000313|Proteomes:UP000014174};
RX PubMed=23846277;
RA Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA Kumar Pinnaka A.;
RT "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT Sample.";
RL Genome Announc. 1:E00484-13(2013).
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:EOR96542.1}.
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DR EMBL; AQPN01000009; EOR96542.1; -; Genomic_DNA.
DR RefSeq; WP_016193523.1; NZ_AQPN01000009.1.
DR AlphaFoldDB; R9GXJ9; -.
DR STRING; 1150600.ADIARSV_0271; -.
DR PATRIC; fig|1150600.3.peg.265; -.
DR eggNOG; COG1619; Bacteria.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000014174; Unassembled WGS sequence.
DR GO; GO:0106415; F:muramoyltetrapeptide carboxypeptidase activity; IEA:UniProtKB-EC.
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:EOR96542.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EOR96542.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000014174};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..128
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 170..286
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 271
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 298 AA; 33038 MW; 53E066688666090A CRC64;
MIAPPYLKKG DKIAITCPAK SLPGDITSAI HLLESWGLEV VIGDTVSASY HQFAGSDELR
TQDMQRFLDD TEIKAIIAAR GGYGTIRIID QLDFSNFTKS PKWLVGFSDI TVLHSHIHAC
CQTQTVHGQM PLNVPDGTKP SLESLRKALF GESLSYQYKS QTTGRNGKTT GTLIGGNLTL
LVMMSGSVSE MDFDDKILFI EDISEYLYSV DRMLWQLKRA GKLAKLKGLI IGDFTDMKDN
STPFGETIPE MVLNHVKEYD YPVCFDFPAG HIADNFALKL GFQIELSVQD LNVSTEQK
//
