NISP_LACLL
ID NISP_LACLL Reviewed; 682 AA.
AC Q07596;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Nisin leader peptide-processing serine protease NisP;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=nisP;
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=8478324; DOI=10.1128/jb.175.9.2578-2588.1993;
RA van der Meer J.R., Polman J., Beerthuyzen M.M., Siezen R.J., Kuipers O.P.,
RA de Vos W.M.;
RT "Characterization of the Lactococcus lactis nisin A operon genes nisP,
RT encoding a subtilisin-like serine protease involved in precursor
RT processing, and nisR, encoding a regulatory protein involved in nisin
RT biosynthesis.";
RL J. Bacteriol. 175:2578-2588(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).
RN [3]
RP 3D-STRUCTURE MODELING.
RX PubMed=7630881; DOI=10.1093/protein/8.2.117;
RA Siezen R.J., Rollema H.S., Kuipers O.P., de Vos W.M.;
RT "Homology modelling of the Lactococcus lactis leader peptidase NisP and its
RT interaction with the precursor of the lantibiotic nisin.";
RL Protein Eng. 8:117-125(1995).
CC -!- FUNCTION: Cleaves the lantibiotic nisin precursor peptide.
CC -!- PATHWAY: Antibiotic biosynthesis; nisin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; L11061; AAA25200.1; -; Genomic_DNA.
DR EMBL; X76884; CAA54210.1; -; Genomic_DNA.
DR PIR; S44131; S44131.
DR RefSeq; WP_014570410.1; NZ_ML956318.1.
DR PDB; 4MZD; X-ray; 1.10 A; A=196-647.
DR PDBsum; 4MZD; -.
DR AlphaFoldDB; Q07596; -.
DR SMR; Q07596; -.
DR MEROPS; S08.059; -.
DR BRENDA; 3.4.22.46; 2864.
DR UniPathway; UPA00853; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07482; Peptidases_S8_Lantibiotic_specific_protease; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR008357; Lanit_process.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PIRSF; PIRSF037875; Peptidase_S8_lp; 1.
DR PRINTS; PR01779; LANTIPROCESS.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Hydrolase; Peptidoglycan-anchor; Protease;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..195
FT /evidence="ECO:0000255"
FT /id="PRO_0000027077"
FT CHAIN 196..655
FT /note="Nisin leader peptide-processing serine protease
FT NisP"
FT /id="PRO_0000027078"
FT PROPEP 656..682
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000027079"
FT DOMAIN 231..566
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT MOTIF 652..656
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT ACT_SITE 259
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 306
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 512
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT MOD_RES 655
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 500
FT /note="A -> T (in Ref. 2; CAA54210)"
FT /evidence="ECO:0000305"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:4MZD"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:4MZD"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 381..397
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 415..423
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:4MZD"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 475..487
FT /evidence="ECO:0007829|PDB:4MZD"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 515..529
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 534..542
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:4MZD"
FT HELIX 556..561
FT /evidence="ECO:0007829|PDB:4MZD"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:4MZD"
SQ SEQUENCE 682 AA; 74768 MW; D5F29313F2983EC9 CRC64;
MKKILGFLFI VCSLGLSATV HGETTNSQQL LSNNINTELI NHNSNAILSS TEGSTTDSIN
LGAQSPAVKS TTRTELDVTG AAKTLLQTSA VQKEMKVSLQ ETQVSSEFSK RDSVTNKEAV
PVSKDELLEQ SEVVVSTSSI QKNKILDNKK KRANFVTSSP LIKEKPSNSK DASGVIDNSA
SPLSYRKAKE VVSLRQPLKN QKVEAQPLLI SNSSEKKASV YTNSHDFWDY QWDMKYVTNN
GESYALYQPS KKISVGIIDS GIMEEHPDLS NSLGNYFKNL VPKGGFDNEE PDETGNPSDI
VDKMGHGTEV AGQITANGNI LGVAPGITVN IYRVFGENLS KSEWVARAIR RAADDGNKVI
NISAGQYLMI SGSYDDGTND YQEYLNYKSA INYATAKGSI VVAALGNDSL NIQDNQTMIN
FLKRFRSIKV PGKVVDAPSV FEDVIAVGGI DGYGNISDFS NIGADAIYAP AGTTANFKKY
GQDKFVSQGY YLKDWLFTTA NTGWYQYVYG NSFATPKVSG ALALVVDKYG IKNPNQLKRF
LLMNSPEVNG NRVLNIVDLL NGKNKAFSLD TDKGQDDAIN HKSMENLKES RDTMKQEQDK
EIQRNTNNNF SIKNDFHNIS KEVISVDYNI NQKMANNRNS RGAVSVRSQE ILPVTGDGED
FLPALGIVCI SILGILKRKT KN
