P2P_LACLC
ID P2P_LACLC Reviewed; 1902 AA.
AC P15293;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=PII-type proteinase;
DE EC=3.4.21.96;
DE AltName: Full=Cell wall-associated serine proteinase;
DE AltName: Full=LP151;
DE AltName: Full=Lactocepin;
DE Flags: Precursor;
GN Name=prt;
OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OG Plasmid pLP763.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 763 / ML3;
RX PubMed=2501630; DOI=10.1111/j.1365-2958.1989.tb00181.x;
RA Kiwaki M., Ikemura H., Shimizu-Kadota M., Hirashima A.;
RT "Molecular characterization of a cell wall-associated proteinase gene from
RT Streptococcus lactis NCDO763.";
RL Mol. Microbiol. 3:359-369(1989).
CC -!- FUNCTION: Protease which breaks down milk proteins during the growth of
CC the bacteria on milk.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase activity with very broad specificity, although
CC some subsite preference have been noted, e.g. large hydrophobic
CC residues in the P1 and P4 positions, and Pro in the P2 position. Best
CC known for its action on caseins, although it has been shown to
CC hydrolyze hemoglobin and oxidized insulin B-chain.; EC=3.4.21.96;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; X14130; CAA32350.1; -; Genomic_DNA.
DR PIR; S06997; S06997.
DR RefSeq; WP_063284091.1; NZ_LITG01000051.1.
DR AlphaFoldDB; P15293; -.
DR SMR; P15293; -.
DR MEROPS; S08.019; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034216; C5a_Peptidase.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR003137; PA_domain.
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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
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.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Cell wall; Hydrolase; Peptidoglycan-anchor; Plasmid; Protease; Repeat;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..187
FT /evidence="ECO:0000255"
FT /id="PRO_0000027089"
FT CHAIN 188..1870
FT /note="PII-type proteinase"
FT /id="PRO_0000027090"
FT PROPEP 1871..1902
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000027091"
FT DOMAIN 191..697
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 1796..1874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1867..1871
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 1830..1868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 281
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 620
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT MOD_RES 1870
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1902 AA; 200140 MW; 4B8D8B844D88CDF7 CRC64;
MQRKKKGLSI LLAGTVALGA LAVLPVGEIQ AKAAISQQTK GSSLANTVTA ATAKQAATDT
TAATTNQAIA TQLAAKGIDY NKLNKVQQQD IYVDVIVQMS AAPASENGTL RTDYSSTAEI
QQETNKVIAA QASVKAAVEQ VTQQTAGESY GYVVNGFSTK VRVVDIPKLK QIAGVKTVTL
AKVYYPTDAK ANSMANVQAV WSNYKYKGEG TVVSVIDSGI DPTHKDMRLS DDKDVKLTKS
DVEKFTDTAK HGRYFNSKVP YGFNYADNND TITDDTVDEQ HGMHVAGIIG ANGTGDDPAK
SVVGVAPEAQ LLAMKVFTNS DTSATTGSAT LVSAIEDSAK IGADVLNMSL GSDSGNQTLE
DPELAAVQNA NESGTAAVIS AGNSGTSGSA TEGVNKDYYG LQDNEMVGTP GTSRGATTVA
SAENTDVITQ AVTITDGTGL QLGPETIQLS SNDFTGSFDQ KKFYVVKDAS GNLSKGKVAD
YTADAKGKIA IVKRGELTFA DKQKYAQAAG AAGLIIVNND GTATPVTSMA LTTTFPTFGL
SSVTGQKLVD WVAAHPDDSL GVKIALTLVP NQKYTEDKMS DFTSYGPVSN LSFKPDITAP
GGNIWSTQNN NGYTNMSGTS MASPFIAGSQ ALLKQALNNK NNPFYAYYKQ LKGTALTDFL
KTVEMNTAQP INDINYNNVI VSPRRQGAGL VDVKAAIDAL EKNPSTVVAE NGYPAVELKD
FTSTDKTFKL TFTNRTTHEL TYQMDSNTDT NAVYTSATDP NSGVLYDKKI DGAAIKAGSN
ITVPAGKTAQ IEFTLSLPKS FDQQQFVEGF LNFKGSDGSR LNLPYMGFFG DWNDGKIVDS
LNGITYSPAG GNFGTVPLLT NKNTGTQYYG GMVTDADGNQ TVDDQAIAFS SDKNALYNDI
SMKYYLLRNI SNVQVDILDG QGNKVTTLSS STNRKKTYYN AHSQQYIYYH APAWDGTYYD
QRDGNIKTAD DGSYTYRISG VPEGGDKRQV FDVPFKLDSK APTVRHVALS AKTENGKTQY
YLTAEAKDDL SGLDATKSVK TAINEVTNLD ATFTDAGTTA DGYTKIETPL SDEQAQALGN
GDNSAELYLT DNASNATDQD ASVQKPGSTS FDLIVNGGGI PDKISSTTTG YEANTQGGGT
YTFSGTYPAA VDGTYTDAQG KKHDLNTTYD AATNSFTASM PVTNADYAAQ VDLYADKAHT
QLLKHFDTKV RLTAPTFTDL KFNNGSDQTS EATIKVTGTV SADTKTVNVG DTVAALDAQH
HFSVDVPVNY GDNTIKVTAT DEDGNTTTEQ KTITSSYDPD MLKNSVTFDQ GVTFGANEFN
ATSAKFYDPK TGIATITGKV KHPTTTLQVD GKQIPIKDDL TFSFTLDLGT LGQKPFGVVV
GDTTQNKTFQ EALTFILDAV APTLSLDSST DAPVYTNNPN FQITGTATDN AQYLSLSING
SSVASQYVDI NINSGKPGHM AIDQPVKLLE GKNVLTVAVT DSEDNTTTKN ITVYYEPKKT
LAAPTVTPST TEPAKTVTLT ANSAATGETV QYSADGGKTY QDVPAAGVTV TANGTFKFKS
TDLYGNESPA VDYVVTNIKA DDPAQLQAAK QELTNLIASA KTLSASGKYD DATTTALAAA
TQKAQTALDQ TNASVDSLTG ANRDLQTAIN QLAAKLPADK KTSLLNQLQS VKAALETDLG
NQTDSSTGKT FTAALDDLVA QAQAGTQTDD QLQATLAKVL DAVLAKLAEG IKAATPAEVG
NAKDAATGKT WYADIADTLT SGQASADASD KLAHLQALQS LKTKVAAAVE AAKTVGKGDG
TTGTSDKGGG QGTPAPTPGD IGKDKGDEGS QPSSGGNIPT NPATTTSTST DDTTDRNGQL
TSGKGALPKT GETTERPAFG FLGVIVVSLM GVLGLKRKQR EE
