ID F5XJ25_MICPN Unreviewed; 343 AA.
AC F5XJ25;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Peptidase S66 family protein {ECO:0000313|EMBL:BAK33351.1};
GN OrderedLocusNames=MLP_03370 {ECO:0000313|EMBL:BAK33351.1};
OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK33351.1, ECO:0000313|Proteomes:UP000007947};
RN [1] {ECO:0000313|EMBL:BAK33351.1, ECO:0000313|Proteomes:UP000007947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA Yamazaki S., Fujita N.;
RT "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL Submitted (MAY-2011) 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; AP012204; BAK33351.1; -; Genomic_DNA.
DR AlphaFoldDB; F5XJ25; -.
DR STRING; 1032480.MLP_03370; -.
DR KEGG; mph:MLP_03370; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_1_1_11; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000007947; 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; cd07062; Peptidase_S66_mccF_like; 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:UP000007947};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 15..134
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 210..326
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
SQ SEQUENCE 343 AA; 36465 MW; C7ABC21DA7580251 CRC64;
MVIRFPAPLS PGDTIAVTSP SSGVAERHRA RLNFAVSTLE ERGYKVIVGN CMDGATHVSA
PAPDRAQELA TFLTDPTVRA VIPPWGGETA IDLLPLLDWD AIAAADPTWF VGFSDISTLI
TPMTLLTGVA TVHGNNLMDT PYRVPDGLIT WLDIATRATG STFTQTSPDR YRSAGWDDYI
AHPEVSEFTL NDPGTWTRLD GSVGDVDVAG RLIGGCIETL CNVTGSPYAD VPKFVSEHAP
EGLLVYVEAS DENAFNICRH LHGMRLAGFF DHANAVLVGR TRAADTPSLT QHEAVLDALG
GLGVPIIGDI ECGHVPPYMP IVNGALGHLR FGGGENSLAQ TLA
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