NISI_LACLL
ID NISI_LACLL Reviewed; 245 AA.
AC P42708;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Nisin immunity protein;
DE Flags: Precursor;
GN Name=nisI;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: Involved in immunity against exogenously supplied nisin.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR EMBL; L16226; AAA25193.1; -; Genomic_DNA.
DR EMBL; X76884; CAA54209.1; -; Genomic_DNA.
DR PIR; S36738; S36738.
DR RefSeq; WP_014570409.1; NZ_ML956318.1.
DR PDB; 2N2E; NMR; -; A=117-245.
DR PDB; 2N32; NMR; -; A=21-129.
DR PDB; 5XHB; X-ray; 1.90 A; A=22-245.
DR PDBsum; 2N2E; -.
DR PDBsum; 2N32; -.
DR PDBsum; 5XHB; -.
DR AlphaFoldDB; P42708; -.
DR BMRB; P42708; -.
DR SMR; P42708; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030153; P:bacteriocin immunity; IEA:UniProtKB-KW.
DR InterPro; IPR040876; Spa1_C.
DR Pfam; PF18218; Spa1_C; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacteriocin immunity; Cell membrane; Lipoprotein; Membrane;
KW Palmitate; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..245
FT /note="Nisin immunity protein"
FT /id="PRO_0000017152"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:5XHB"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 57..71
FT /evidence="ECO:0007829|PDB:5XHB"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 85..96
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:5XHB"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:5XHB"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2N32"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2N2E"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:5XHB"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 169..183
FT /evidence="ECO:0007829|PDB:5XHB"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:5XHB"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2N2E"
FT STRAND 209..220
FT /evidence="ECO:0007829|PDB:5XHB"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:5XHB"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:5XHB"
SQ SEQUENCE 245 AA; 27837 MW; 72DCE887DBB0E30C CRC64;
MRRYLILIVA LIGITGLSGC YQTSHKKVRF DEGSYTNFIY DNKSYFVTDK EIPQENVNNS
KVKFYKLLIV DMKSEKLLSS SNKNSVTLVL NNIYEASDKS LCMGINDRYY KILPESDKGA
VKALRLQNFD VTSDISDDNF VIDKNDSRKI DYMGNIYSIS DTTVSDEELG EYQDVLAEVR
VFDSVSGKSI PRSEWGRIDK DGSNSKQSRT EWDYGEIHSI RGKSLTEAFA VEINDDFKLA
TKVGN