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MCCF_ECOLX
ID   MCCF_ECOLX              Reviewed;         344 AA.
AC   Q47511;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Microcin C7 self-immunity protein MccF;
GN   Name=mccF;
OS   Escherichia coli.
OG   Plasmid pMccC7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8522520; DOI=10.1128/jb.177.24.7131-7140.1995;
RA   Gonzalez-Pastor J.E., San Millan J.L., Castilla M.A., Moreno F.;
RT   "Structure and organization of plasmid genes required to produce the
RT   translation inhibitor microcin C7.";
RL   J. Bacteriol. 177:7131-7140(1995).
CC   -!- FUNCTION: Involved in specific self-immunity to microcin C7.
CC   -!- INTERACTION:
CC       Q47511; Q47511: mccF; NbExp=2; IntAct=EBI-15973002, EBI-15973002;
CC   -!- SIMILARITY: Belongs to the peptidase S66 family. {ECO:0000305}.
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DR   EMBL; X57583; CAA40814.1; -; Genomic_DNA.
DR   RefSeq; WP_000973426.1; NZ_VRXN01000031.1.
DR   PDB; 3TLA; X-ray; 1.20 A; A/B=2-344.
DR   PDB; 3TLB; X-ray; 1.50 A; A/B=2-344.
DR   PDB; 3TLC; X-ray; 1.30 A; A/B=2-344.
DR   PDB; 3TLE; X-ray; 1.30 A; A/B=2-344.
DR   PDB; 3TLG; X-ray; 1.50 A; A/B=2-344.
DR   PDB; 3TLY; X-ray; 1.70 A; A/B=2-344.
DR   PDB; 3TLZ; X-ray; 1.50 A; A/B=2-344.
DR   PDB; 4IIX; X-ray; 1.23 A; A/B=2-344.
DR   PDB; 4IIY; X-ray; 1.20 A; A/B=2-344.
DR   PDBsum; 3TLA; -.
DR   PDBsum; 3TLB; -.
DR   PDBsum; 3TLC; -.
DR   PDBsum; 3TLE; -.
DR   PDBsum; 3TLG; -.
DR   PDBsum; 3TLY; -.
DR   PDBsum; 3TLZ; -.
DR   PDBsum; 4IIX; -.
DR   PDBsum; 4IIY; -.
DR   AlphaFoldDB; Q47511; -.
DR   SMR; Q47511; -.
DR   DIP; DIP-60028N; -.
DR   ChEMBL; CHEMBL3596082; -.
DR   MEROPS; S66.003; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0030153; P:bacteriocin immunity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10740; -; 1.
DR   Gene3D; 3.50.30.60; -; 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; PTHR30237; 1.
DR   Pfam; PF02016; Peptidase_S66; 1.
DR   Pfam; PF17676; Peptidase_S66C; 1.
DR   PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR   SUPFAM; SSF141986; SSF141986; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bacteriocin immunity; Hydrolase; Plasmid.
FT   CHAIN           1..344
FT                   /note="Microcin C7 self-immunity protein MccF"
FT                   /id="PRO_0000172840"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           28..31
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           33..45
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   TURN            54..57
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           67..79
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           95..101
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           104..109
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           121..131
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           141..145
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           151..164
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          203..206
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          208..218
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           219..222
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   TURN            223..227
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          239..243
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           249..261
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           264..266
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          269..274
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   HELIX           288..296
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          303..308
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          310..314
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          318..327
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   TURN            328..331
FT                   /evidence="ECO:0007829|PDB:4IIY"
FT   STRAND          332..335
FT                   /evidence="ECO:0007829|PDB:4IIY"
SQ   SEQUENCE   344 AA;  38361 MW;  759CEF7AB49E5C2D CRC64;
     MMIQSHPLLA APLAVGDTIG FFSSSAPATV TAKNRFFRGV EFLQRKGFKL VSGKLTGKTD
     FYRSGTIKER AQEFNELVYN PDITCIMSTI GGDNSNSLLP FLDYDAIIAN PKIIIGYSDT
     TALLAGIYAK TGLITFYGPA LIPSFGEHPP LVDITYESFI KILTRKQSGI YTYTLPEKWS
     DESINWNENK ILRPKKLYKN NCAFYGSGKV EGRVIGGNLN TLTGIWGSEW MPEILNGDIL
     FIEDSRKSIA TIERLFSMLK LNRVFDKVSA IILGKHELFD CAGSKRRPYE VLTEVLDGKQ
     IPVLDGFDCS HTHPMLTLPL GVKLAIDFDN KNISITEQYL STEK
 
 
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