NISC_LACLL
ID NISC_LACLL Reviewed; 418 AA.
AC Q03202;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Nisin biosynthesis protein NisC;
GN Name=nisC;
OS Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1360;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=6F3;
RX PubMed=1482192; DOI=10.1128/aem.58.11.3730-3743.1992;
RA Engelke G., Gutowski-Eckel Z., Hammelmann M., Entian K.-D.;
RT "Biosynthesis of the lantibiotic nisin: genomic organization and membrane
RT localization of the NisB protein.";
RL Appl. Environ. Microbiol. 58:3730-3743(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NIZO R5;
RX PubMed=7689965; DOI=10.1111/j.1432-1033.1993.tb18143.x;
RA Kuipers O.P., Beerthuyzen M.M., Siezen R.J., de Vos W.M.;
RT "Characterization of the nisin gene cluster nisABTCIPR of Lactococcus
RT lactis. Requirement of expression of the nisA and nisI genes for
RT development of immunity.";
RL Eur. J. Biochem. 216:281-291(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 397-418.
RC STRAIN=6F3;
RX PubMed=8161176; DOI=10.1128/aem.60.3.814-825.1994;
RA Engelke G., Gutowski-Eckel Z., Kiesau P., Siegers K., Hammelmann M.,
RA Entian K.-D.;
RT "Regulation of nisin biosynthesis and immunity in Lactococcus lactis 6F3.";
RL Appl. Environ. Microbiol. 60:814-825(1994).
CC -!- FUNCTION: Could be implicated in the processing or the export process
CC of the nisin lantibiotic.
CC -!- SIMILARITY: To B.subtilis SpaC and S.epidermidis EpiC. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X68307; CAA48383.1; -; Genomic_DNA.
DR EMBL; L16226; AAA25192.1; ALT_INIT; Genomic_DNA.
DR PIR; D48951; D48951.
DR RefSeq; WP_043991124.1; NZ_ML956318.1.
DR PDB; 2G02; X-ray; 2.50 A; A=7-415.
DR PDB; 2G0D; X-ray; 2.21 A; A=7-415.
DR PDBsum; 2G02; -.
DR PDBsum; 2G0D; -.
DR AlphaFoldDB; Q03202; -.
DR SMR; Q03202; -.
DR EvolutionaryTrace; Q03202; -.
DR CDD; cd04793; LanC; 1.
DR InterPro; IPR033889; LanC.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR020468; Nisin_biosynthesis_NisC.
DR Pfam; PF05147; LANC_like; 1.
DR PRINTS; PR01950; LANCSUPER.
DR PRINTS; PR01952; NISCPROTEIN.
DR SMART; SM01260; LANC_like; 1.
PE 1: Evidence at protein level;
KW 3D-structure.
FT CHAIN 1..418
FT /note="Nisin biosynthesis protein NisC"
FT /id="PRO_0000096864"
FT HELIX 9..26
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:2G0D"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:2G0D"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 59..80
FT /evidence="ECO:0007829|PDB:2G0D"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2G0D"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 106..128
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:2G0D"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:2G0D"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2G0D"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:2G0D"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2G0D"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 232..248
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:2G0D"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:2G0D"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 304..320
FT /evidence="ECO:0007829|PDB:2G0D"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 333..347
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 353..361
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 363..368
FT /evidence="ECO:0007829|PDB:2G0D"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 382..393
FT /evidence="ECO:0007829|PDB:2G0D"
FT HELIX 401..405
FT /evidence="ECO:0007829|PDB:2G0D"
FT TURN 409..413
FT /evidence="ECO:0007829|PDB:2G0D"
SQ SEQUENCE 418 AA; 47931 MW; F3187AE5370A94DF CRC64;
MRIMMNKKNI KRNVEKIIAQ WDERTRKNKE NFDFGELTLS TGLPGIILML AELKNKDNSK
IYQKKIDNYI EYIVSKLSTY GLLTGSLYSG AAGIALSILH LREDDEKYKN LLDSLNRYIE
YFVREKIEGF NLENITPPDY DVIEGLSGIL SYLLLINDEQ YDDLKILIIN FLSNLTKENN
GLISLYIKSE NQMSQSESEM YPLGCLNMGL AHGLAGVGCI LAYAHIKGYS NEASLSALQK
IIFIYEKFEL ERKKQFLWKD GLVADELKKE KVIREASFIR DAWCYGGPGI SLLYLYGGLA
LDNDYFVDKA EKILESAMQR KLGIDSYMIC HGYSGLIEIC SLFKRLLNTK KFDSYMEEFN
VNSEQILEEY GDESGTGFLE GISGCILVLS KFEYSINFTY WRQALLLFDD FLKGGKRK
