ID M1PCM7_DESSD Unreviewed; 311 AA.
AC M1PCM7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative MccF-like protein (Microcin C7 resistance) {ECO:0000313|EMBL:AGF79367.1};
GN OrderedLocusNames=UWK_02836 {ECO:0000313|EMBL:AGF79367.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF79367.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP003985; AGF79367.1; -; Genomic_DNA.
DR RefSeq; WP_015405053.1; NC_020304.1.
DR AlphaFoldDB; M1PCM7; -.
DR STRING; 1167006.UWK_02836; -.
DR KEGG; dsf:UWK_02836; -.
DR PATRIC; fig|1167006.5.peg.3064; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_3_1_7; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000011721; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000011721};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 17..134
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 178..296
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 209
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 311 AA; 34773 MW; 1468C31569C07CEE CRC64;
MTYNSRLPAP LQPGDCIGII APAGQIHDTK PLEQGMAILQ NMGFELRLPR NLWPGKGYLA
DSDANRALEF HRMWSDPEIS ALLALRGGFG SLRLLPFLNP EDIKKERKLL IGFSDITILH
SAIHQTNDLI TLHGPMLTTL SSISSDSLQH FYACLSGNWD KPLQNHQIEV LRDGPPVRGK
LIGGNLSSLI SILATAIDQD WSKKIVFLED VGEPLYRLDR MFTQLWHSGK INQPAGIILG
DFSINQEQDS LEKIRFHEEI WKRVLELTEA AGMPVWGNFP IGHGRNNLTM PHGADALMDS
NAVRLSYPHR P
//
