ID A0A172ZGK0_9BACL Unreviewed; 362 AA.
AC A0A172ZGK0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Microcin immunity protein {ECO:0000313|EMBL:ANF96775.1};
GN ORFNames=AR543_12655 {ECO:0000313|EMBL:ANF96775.1};
OS Paenibacillus bovis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF96775.1, ECO:0000313|Proteomes:UP000078148};
RN [1] {ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA Wu Z., Gao C., Liu Z., Zheng H.;
RT "Genome of Paenibacillus bovis sp. nov.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANF96775.1, ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|EMBL:ANF96775.1,
RC ECO:0000313|Proteomes:UP000078148};
RX PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT milk.";
RL Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP013023; ANF96775.1; -; Genomic_DNA.
DR RefSeq; WP_060534880.1; NZ_CP013023.1.
DR AlphaFoldDB; A0A172ZGK0; -.
DR STRING; 1616788.AR543_12655; -.
DR KEGG; pbv:AR543_12655; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000078148; 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:UP000078148};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 34..154
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 226..346
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 134
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 266
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 362 AA; 40096 MW; DBCD9188D181D792 CRC64;
MEYIPDRYSS ADNGFSYPSS QIIYPAPLRK GDRIAIIAPS SGVNPEAHHL LHRTREYLEQ
LGYMVTLGDS VWTNDKCVSL PKAERAAELQ QFLLDEQVQA IIPPWGGEFL MELLPLLDWD
RIREQPPKWI LGFSDISTLT FAYTLQTGYA SAHGPGAIDI SGSDDPTTSI WLQMLTAADG
QSVEQYSSTH YQTVSDHSQP GYNLDTSTEW RILGQEDQPE ASLQFSGRLI GGCMDVITVL
IGTKWAPVNE FIEHYAASDS VIWYLESCEM NAGDIYRHLW QMDQAGWFRH AKGILIGRPA
GYSALGNFEL TDALQQVFGD RNIPVVYGVD IGHIPPQLTL INGASAIVSV KSGQGSIVQT
LD
//
