CCLA_CARML
ID CCLA_CARML Reviewed; 64 AA.
AC B2MVM5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Carnocyclin-A;
DE Flags: Precursor;
GN Name=cclA {ECO:0000312|EMBL:ACC93994.1};
OS Carnobacterium maltaromaticum (Carnobacterium piscicola).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=2751;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACC93994.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-64, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=UAL307 {ECO:0000312|EMBL:ACC93994.1};
RX PubMed=18552180; DOI=10.1128/aem.00817-08;
RA Martin-Visscher L.A., van Belkum M.J., Garneau-Tsodikova S., Whittal R.M.,
RA Zheng J., McMullen L.M., Vederas J.C.;
RT "Isolation and characterization of carnocyclin a, a novel circular
RT bacteriocin produced by Carnobacterium maltaromaticum UAL307.";
RL Appl. Environ. Microbiol. 74:4756-4763(2008).
CC -!- FUNCTION: Cyclopeptide antibiotic that inhibits the growth of Gram-
CC positive bacteria, but has no effect on the growth of Gram-negative
CC bacteria. {ECO:0000269|PubMed:18552180}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Stable from pH 2 to 12. {ECO:0000269|PubMed:18552180};
CC Temperature dependence:
CC Displays a high degree of stability when incubated at temperatures
CC between -80 and 75 degrees Celsius for 60 minutes. Autoclaving the
CC peptide at 121 degrees Celsius for 15 minutes had no effect but
CC incubation at 100 degrees Celsius for 60 minutes caused a 32-fold
CC reduction in activity. {ECO:0000269|PubMed:18552180};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18552180}.
CC -!- MASS SPECTROMETRY: Mass=5862; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18552180};
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DR EMBL; EU624394; ACC93994.1; -; Genomic_DNA.
DR PDB; 2KJF; NMR; -; A=5-64.
DR PDBsum; 2KJF; -.
DR AlphaFoldDB; B2MVM5; -.
DR BMRB; B2MVM5; -.
DR SMR; B2MVM5; -.
DR TCDB; 1.C.90.1.1; the carnocyclin a (carnocyclin) family.
DR EvolutionaryTrace; B2MVM5; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR Gene3D; 1.20.225.10; -; 1.
DR InterPro; IPR009086; Bacteriocin_AS48.
DR InterPro; IPR020038; Circ_bacteriocin.
DR Pfam; PF09221; Bacteriocin_IId; 1.
DR TIGRFAMs; TIGR03651; circ_ocin_uber; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW Direct protein sequencing; Secreted.
FT PROPEP 1..4
FT /evidence="ECO:0000269|PubMed:18552180"
FT /id="PRO_0000361696"
FT PEPTIDE 5..64
FT /note="Carnocyclin-A"
FT /id="PRO_0000361697"
FT CROSSLNK 5..64
FT /note="Cyclopeptide (Leu-Leu)"
FT /evidence="ECO:0000269|PubMed:18552180"
FT CONFLICT 32
FT /note="I -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:2KJF"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:2KJF"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:2KJF"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:2KJF"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2KJF"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:2KJF"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:2KJF"
SQ SEQUENCE 64 AA; 6417 MW; 141B4BEF7FE9E56C CRC64;
MLYELVAYGI AQGTAEKVVS LINAGLTVGS IISILGGVTV GLSGVFTAVK AAIAKQGIKK
AIQL
