ID A0A059NZI5_9BACI Unreviewed; 325 AA.
AC A0A059NZI5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Microcin C7 self-immunity protein MccF {ECO:0000313|EMBL:CDQ24777.1};
GN Name=mccF {ECO:0000313|EMBL:CDQ24777.1};
GN ORFNames=BN983_03074 {ECO:0000313|EMBL:CDQ24777.1};
OS Halobacillus karajensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=195088 {ECO:0000313|EMBL:CDQ24777.1, ECO:0000313|Proteomes:UP000028868};
RN [1] {ECO:0000313|EMBL:CDQ24777.1, ECO:0000313|Proteomes:UP000028868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ24777.1,
RC ECO:0000313|Proteomes:UP000028868};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDQ24777.1, ECO:0000313|Proteomes:UP000028868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ24777.1,
RC ECO:0000313|Proteomes:UP000028868};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Halobacillus karajensis HK-03.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:CDQ24777.1}.
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DR EMBL; CCDI010000004; CDQ24777.1; -; Genomic_DNA.
DR RefSeq; WP_035509993.1; NZ_CCDJ010000003.1.
DR AlphaFoldDB; A0A059NZI5; -.
DR Proteomes; UP000028868; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; 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:SF5; CARBOXYPEPTIDASE YOCD-RELATED; 1.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000028868}.
FT DOMAIN 12..131
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 197..311
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 325 AA; 36792 MW; EF95F3F2B94DE08A CRC64;
MIPKKLRKGN EIRILSPAKS LSMIDQDQQK LAVRRLNDAG FQVTFGTYAA EEYNHISTPV
DHRVNDIHDA FADPNVKAIL TTIGGYDSNQ LLSDLDYQVI RQNPKIFCGY SDITALSNSI
YRKTGLVTYS GPHFSSFGME QGIDYTYEFF LKVCREKDPF NIPPAESWSD DHWYLDQENR
QFHKNNGYNV INEGIAEGTS IGGNLCTLNL LQGTEFMPSL EDTILFLEDD LLSDAPTFDR
NLQSLIHQPG FYGVKGIIIG RFQKDSKVKD RDLQQIIQSK KELTTIPVIS NASFGHTTPI
FTFPIGGQVK MKAYNHDTTI ELLKY
//
