ID A5CCE4_ORITB Unreviewed; 332 AA.
AC A5CCE4;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Microcin C7 self-immunity protein {ECO:0000313|EMBL:CAM79343.1};
DE EC=3.4.17.13 {ECO:0000313|EMBL:CAM79343.1};
GN Name=mccF {ECO:0000313|EMBL:CAM79343.1};
GN OrderedLocusNames=OTBS_0277 {ECO:0000313|EMBL:CAM79343.1};
OS Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=357244 {ECO:0000313|EMBL:CAM79343.1, ECO:0000313|Proteomes:UP000001565};
RN [1] {ECO:0000313|EMBL:CAM79343.1, ECO:0000313|Proteomes:UP000001565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boryong {ECO:0000313|EMBL:CAM79343.1,
RC ECO:0000313|Proteomes:UP000001565};
RX PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT "The Orientia tsutsugamushi genome reveals massive proliferation of
RT conjugative type IV secretion system and host-cell interaction genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; AM494475; CAM79343.1; -; Genomic_DNA.
DR RefSeq; WP_011944378.1; NC_009488.1.
DR AlphaFoldDB; A5CCE4; -.
DR KEGG; ots:OTBS_0277; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_3_1_5; -.
DR OMA; GFIFGQC; -.
DR Proteomes; UP000001565; Chromosome.
DR GO; GO:0106415; F:muramoyltetrapeptide carboxypeptidase activity; IEA:UniProtKB-EC.
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:CAM79343.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAM79343.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001565};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 26..150
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 201..310
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 131
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 231
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 332 AA; 37594 MW; CD8072DB9B5A797E CRC64;
MRFIILLFSF VVASVSICFA IPDTIIDVIA PSSKGSELNL QLIEDYLESI GVKANVPENI
YSDNEPLYSN TDEFRAESLV KALTNPKSIA IWCIRGGRGA SRLIPYLEKL PDDVKKKIAQ
NKNRKILMGF SDVSVLHIYL QNKYDWSTLH SPMLEQIVDN KISQDSIDKL ELLISGYRNN
IKFNLKMIDN GIELNDGILE SKVVGGSISL VRASIGTCWQ IDTKDKILFL EEVEPDPALL
EMRLEHLKQA HILDEVQAVI FGDILCTNDE QLLELVKHRF AQSVNFPVFT LNGIGHARTN
YPLPLNTRAV INHIKGNRFS MTVDMPAEWR RR
//