ID   MACM_STRMA              Reviewed;         144 AA.
AC   P01549;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Macromomycin;
DE            Short=MCR;
DE   AltName: Full=Auromomycin apoprotein;
DE   Flags: Precursor;
OS   Streptomyces macromomyceticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M480-M1;
RX   PubMed=2479629; DOI=10.7164/antibiotics.42.1704;
RA   Sakata N., Kanbe T., Tanabe M., Hayashi H., Hori M., Hotta K., Hamada M.;
RT   "Nucleotide sequence of the macromomycin apoprotein gene and its expression
RT   in Streptomyces macromomyceticus.";
RL   J. Antibiot. 42:1704-1712(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-144.
RX   PubMed=6848492; DOI=10.1016/s0021-9258(18)33238-1;
RA   Samy T.S.A., Hahm K.-S., Modest E.J., Lampman G.W., Keutmann H.T.,
RA   Umezawa H., Herlihy W.C., Gibson B.W., Carr S.A., Biemann K.;
RT   "Primary structure of macromomycin, an antitumor antibiotic protein.";
RL   J. Biol. Chem. 258:183-191(1983).
RN   [3]
RP   PROTEIN SEQUENCE OF 33-78.
RX   PubMed=155453; DOI=10.1016/0006-291x(79)90235-3;
RA   Sawyer T.H., Guetzow K., Olson M.O.J., Busch H., Prestayko A.W.,
RA   Crooke S.T.;
RT   "Amino terminal amino acid sequence of macromomycin, a protein antitumor
RT   antibiotic.";
RL   Biochem. Biophys. Res. Commun. 86:1133-1138(1979).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=2771945; DOI=10.1073/pnas.86.17.6587;
RA   van Roey P., Beerman T.A.;
RT   "Crystal structure analysis of auromomycin apoprotein (macromomycin) shows
RT   importance of protein side chains to chromophore binding selectivity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:6587-6591(1989).
CC   -!- FUNCTION: Binds non-covalently to a chromophore which is the cytotoxic
CC       and mutagenic component of the antibiotic. The chromophore binds to DNA
CC       as a weak intercalator and causes single- and double-strand breaks.
CC   -!- SIMILARITY: Belongs to the neocarzinostatin family. {ECO:0000305}.
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DR   EMBL; D90006; BAA14059.1; -; Genomic_DNA.
DR   PIR; A45766; YMSMCM.
DR   PDB; 2MCM; X-ray; 1.50 A; A=33-144.
DR   PDBsum; 2MCM; -.
DR   AlphaFoldDB; P01549; -.
DR   SMR; P01549; -.
DR   EvolutionaryTrace; P01549; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR027273; Neocarzinostatin-like.
DR   InterPro; IPR002186; Neocarzinostatin_fam.
DR   Pfam; PF00960; Neocarzinostat; 1.
DR   PRINTS; PR01885; MACROMOMYCIN.
DR   SUPFAM; SSF49319; SSF49319; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Disulfide bond; DNA-binding; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000269|PubMed:155453,
FT                   ECO:0000269|PubMed:6848492"
FT   CHAIN           33..144
FT                   /note="Macromomycin"
FT                   /id="PRO_0000019460"
FT   DISULFID        68..78
FT                   /evidence="ECO:0000269|PubMed:6848492"
FT   DISULFID        120..125
FT                   /evidence="ECO:0000269|PubMed:6848492"
FT   CONFLICT        48
FT                   /note="Q -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="Missing (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67..68
FT                   /note="QC -> ES (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="V -> A (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78
FT                   /note="C -> P (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          35..40
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   STRAND          48..56
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   STRAND          62..72
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   TURN            80..82
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   STRAND          94..100
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   STRAND          102..108
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   TURN            109..112
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   STRAND          113..119
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   TURN            120..122
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   STRAND          125..130
FT                   /evidence="ECO:0007829|PDB:2MCM"
FT   STRAND          136..141
FT                   /evidence="ECO:0007829|PDB:2MCM"
SQ   SEQUENCE   144 AA;  13967 MW;  18023F50BF3079EE CRC64;
     MLQNTSRFLA RAGATVGVAA GLAFSLPADR DGAPGVTVTP ATGLSNGQTV TVSATGLTPG
     TVYHVGQCAV VEPGVIGCDA TTSTDVTADA AGKITAQLKV HSSFQAVVGA NGTPWGTVNC
     KVVSCSAGLG SDSGEGAAQA ITFA