KEDA_ACTSL
ID KEDA_ACTSL Reviewed; 114 AA.
AC P41249;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Apokedarcidin;
OS Actinomycete sp. (strain L585-6 / ATCC 53650).
OC Bacteria; Actinobacteria; Actinomycetales.
OX NCBI_TaxID=38989;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 53650 / L585-6;
RX PubMed=1399845; DOI=10.7164/antibiotics.45.1250;
RA Hofstead S.J., Matson J.A., Malacko A.R., Marquardt H.;
RT "Kedarcidin, a new chromoprotein antitumor antibiotic. II. Isolation,
RT purification and physico-chemical properties.";
RL J. Antibiot. 45:1250-1254(1992).
RN [2]
RP CHARACTERIZATION.
RX PubMed=8367457; DOI=10.1073/pnas.90.17.8009;
RA Zein N., Casazza A.M., Doyle T.W., Leet J.E., Scheoeder D.R., Solomon W.,
RA Nadler S.G.;
RT "Selective proteolytic activity of the antitumor agent kedarcidin.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8009-8012(1993).
RN [3]
RP STRUCTURE BY NMR.
RC STRAIN=ATCC 53650 / L585-6;
RX PubMed=7918358; DOI=10.1021/bi00204a006;
RA Constantine K.L., Colson K.L., Wittekind M., Friedrichs M.S., Zein N.,
RA Tuttle J., Langley D.R., Leet J.E., Schroeder D.R., Lam K.S.,
RA Farmer B.T. II, Metzler W.J., Bruccoleri R.E., Mueller L.;
RT "Sequential 1H, 13C, and 15N NMR assignments and solution conformation of
RT apokedarcidin.";
RL Biochemistry 33:11438-11452(1994).
CC -!- FUNCTION: Binds non-covalently to an enediyne chromophore which is the
CC cytotoxic and mutagenic component of the antibiotic. The chromophore
CC cleaves duplex DNA site-specifically in a single-stranded manner. The
CC apoprotein cleaves proteins selectively, in particular highly basic
CC histones, with H1 proteins being cleaved the more readily.
CC -!- DOMAIN: This protein consists of an immunoglobulin-like seven-stranded
CC antiparallel beta-barrel domain linked to a subdomain composed of two
CC beta-hairpin ribbons.
CC -!- SIMILARITY: Belongs to the neocarzinostatin family. {ECO:0000305}.
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DR PDB; 1AKP; NMR; -; A=1-114.
DR PDBsum; 1AKP; -.
DR AlphaFoldDB; P41249; -.
DR BMRB; P41249; -.
DR SMR; P41249; -.
DR EvolutionaryTrace; P41249; -.
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.
FT CHAIN 1..114
FT /note="Apokedarcidin"
FT /id="PRO_0000213119"
FT DISULFID 37..47
FT /evidence="ECO:0000269|PubMed:7918358,
FT ECO:0007744|PDB:1AKP"
FT DISULFID 88..95
FT /evidence="ECO:0000269|PubMed:7918358,
FT ECO:0007744|PDB:1AKP"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1AKP"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1AKP"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1AKP"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1AKP"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1AKP"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1AKP"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1AKP"
FT STRAND 84..97
FT /evidence="ECO:0007829|PDB:1AKP"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1AKP"
SQ SEQUENCE 114 AA; 10969 MW; 1901E2B14E4197B4 CRC64;
ASAAVSVSPA TGLADGATVT VSASGFATST SATALQCAIL ADGRGACNVA EFHDFSLSGG
EGTTSVVVRR SFTGYVMPDG PEVGAVDCDT APGGCEIVVG GNTGEYGNAA ISFG
