ID A0A1M7QC43_9BACT Unreviewed; 348 AA.
AC A0A1M7QC43;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SHN28390.1};
GN ORFNames=SAMN04488057_11655 {ECO:0000313|EMBL:SHN28390.1};
OS Cyclobacterium lianum.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=388280 {ECO:0000313|EMBL:SHN28390.1, ECO:0000313|Proteomes:UP000184513};
RN [1] {ECO:0000313|EMBL:SHN28390.1, ECO:0000313|Proteomes:UP000184513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6102 {ECO:0000313|EMBL:SHN28390.1,
RC ECO:0000313|Proteomes:UP000184513};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; FRCY01000016; SHN28390.1; -; Genomic_DNA.
DR RefSeq; WP_073097100.1; NZ_FRCY01000016.1.
DR AlphaFoldDB; A0A1M7QC43; -.
DR STRING; 388280.SAMN04488057_11655; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000184513; 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:SHN28390.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000184513};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 46..163
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 217..332
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 143
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 248
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 318
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 348 AA; 38213 MW; 0B486E337187B679 CRC64;
MEKREFIKSL GLGLGLMPLS GLAKTTEKQP SQDRLLPKKL QPGDQVGLVS PSAATADIME
FTFAREALEA LGLKVEQGKY LKERRGHLAG TDAERAADIN EMFGNKRIKA IVCIRGGSGA
ARILPLLDYE LIRKNPKPIM GYSDITALHN AINAQTGLIT FHGPNGSGSW NNFNANQFRS
VFFGTGETIT YKNESEETED LVNKKNRIRT IYPGKAEGSL VGGNLTVLTA LAGSPYLPDF
RGKLLFLEDI GEEPYRIDRM MSTLMLMGVF RQISGFVFGQ CTDCDPGGGY GNLTLDQIFD
DYLLPHKIPA FRGAMIGHIP SQFLLPFGAK MAMDANRGIL ETREALFQ
//
