P2P_LACPA
ID P2P_LACPA Reviewed; 1902 AA.
AC Q02470;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=prtP;
OS Lacticaseibacillus paracasei (Lactobacillus paracasei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25302 / DSM 5622 / BCRC 12248 / JCM 8130 / KCTC 3510 / LMG
RC 13087 / NBRC 15889 / NCDO 151 / RO94;
RX PubMed=1512565; DOI=10.1099/00221287-138-7-1353;
RA Holck A., Naes H.;
RT "Cloning, sequencing and expression of the gene encoding the cell-envelope-
RT associated proteinase from Lactobacillus paracasei subsp. paracasei NCDO
RT 151.";
RL J. Gen. Microbiol. 138:1353-1364(1992).
RN [2]
RP PROTEIN SEQUENCE OF 189-196.
RX PubMed=1564442; DOI=10.1099/00221287-138-2-313;
RA Naes H., Nissen-Meyer J.;
RT "Purification and N-terminal amino acid sequence determination of the cell-
RT wall-bound proteinase from Lactobacillus paracasei subsp. paracasei.";
RL J. Gen. Microbiol. 138:313-318(1992).
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; M83946; AAA25248.1; -; Genomic_DNA.
DR PIR; B44858; B44858.
DR RefSeq; WP_003661853.1; NZ_JACEIM010000004.1.
DR AlphaFoldDB; Q02470; -.
DR SMR; Q02470; -.
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 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; Hydrolase; Peptidoglycan-anchor;
KW Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..187
FT /evidence="ECO:0000255"
FT /id="PRO_0000027092"
FT CHAIN 188..1870
FT /note="PII-type proteinase"
FT /id="PRO_0000027093"
FT PROPEP 1871..1902
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000027094"
FT DOMAIN 191..697
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 1793..1872
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 1828..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; 200253 MW; D8C9F38CEE5DA582 CRC64;
MQRKKKGLSI LLAGTVALGA LAVLPVGEIQ AKAAISQQTK VSSLANTVKA ATAKQAATDT
TAATTNQAIA TQLAAKGIDY NKLNKVQQQD TYVDVIVQMS AAPASENGTL RTDYSSTAEI
QQETNKVIAA QASVKAAVEQ VTQQTAGESY GYVVNGFSTK VRVVDIPKLK QIAGVKTVTL
AKVYYPTDAK ANSMANVQAV WSNYKYKGEG TVVSVIDTGI DPTHKDMRLS DDKDVKLTKY
DVEKFTDTAK HGRYFTSKVP YGFNYADNND TITDDTVDEQ HGMHVAGIIG ANGTGDDPTK
SVVGVAPEAQ LLAMKVFTNS DTSATTGSAT LVSAIEDSAK IGADVLNMSL GSDSGNQTLE
DPEIAAVQNA NESGTAAVIS AGNSGTSGSA TQGVNKDYYG LQDNEMVGTP GTSRGATTVA
SAENTDVISQ AVTITDGKDL QLGPETIQLS SNDFTGSFDQ KKFYVVKDAS GDLSKGAAAD
YTADAKGKIA IVKRGELNFA DKQKYAQAAG AAGLIIVNND GTATPLTSIR LTTTFPTFGL
SSKTGQKLVD WVTAHPDDSL GVKIALTLLP NQKYTEDKMS DFTSYGPVSN LSFKPDITAP
GGNIWSTQNN NGYTNMSGTS MASPFIAGSQ ALLKQALNNK NNPFYADYKQ LKGTALTDFL
KTVEMNTAQP INDINYNNVI VSPRRQGAGL VDVKAAIDAL EKNPSTVVAE NGYPAVELKD
FTSTDKTFKL TFTNRTTHEL TYQMDSNTDT NAVYTSATDP NSGVLYDKKI DGAAIKAGSD
ITVPAGKTAQ IEFTLSLPKS FDQQQFVEGF LNFKGSDGSR LNLPYMGFFG DWNDGKIVDS
LNGITYSPAG GNYGTVPLLT NKNTGHQYYG GMVTDADGKQ TVDDQAIAFS SDKNALYNDI
SMQYYLLRNI SNVQVDILDG QGNKVTTLSS STNQTKTYYD AHSQKYIYYN APAWDGTYYD
QRDGNIKTAD DGSYTYRISG VPEGGDKRQV FDVPFKLDSK APTVRHVALS AKTENGKTQY
YLTAEAKDDL SGLDATKSVK TAINEVTNLD ATFTDAGTTA DGYTKIETPL SDEQAQALGN
GDNSAELYLT DNASNATNQD ASVQKPGSTS FDLIVNGGGI PDKISSTTTG YEANTQGGGT
YTFSGTYPAA VDGTYTDAQG KKHDLNTTYD AATNSFTASM AVTNADYAAQ VDLYADKAHT
QLLKHFDTKV RLTAPTFTDL KFNNGSDQTS EATIKVTGTV SSDTKTVNVG DTVAALDAQH
HFSVDVPVNY GDNTIKVTAT DEDGNTTTEQ KTITSSYDPD VLKNAVTFDQ GVKFGANEFN
ATSAKFYDPK TGIATITGKV KHPTTTLQVD GKQISIKNDL TFSFTLDLGT LGQKPFGVVV
GDTTQNKTFQ EALTFILDAV APTLSLDSST DAPVYTNDPN FQITGTATDN AQYLSLAING
SHVASQYADI NINSGKPGHM AIDQPVKLLE GKNVLTVAVT DSENNTTTKK ITVYYEPKKT
LAAPTVTPST TEPAKTVTLT ANAAATGETV QYSADGGKTY QDVPAAGVTV TANGTFKFKS
TDLYGNESPA VDYVVTNIKA DDPAQLQTAK QALTNLIASA KTLSASGKYD DATTTALAAA
TQKAQTALDQ TDASVDSLTG ANRDLQTAIN QLAAKLPADK KTSLLNQLQS VKAALGTDLG
NQTDPSTGKT FTAALDDLVA QAQAGTQTAD QLQASLAKVL DAVLAKLAEG IKAATPAEVG
NAKDAATGKT WYADIADTLT SGQASADASD KLAHLQALQS LKTKVAAAVE AAKTAGKGDD
TTGTSDKGGG QGTPAPAPGD TGKDKGDEGS QPSSGGNIPT KPATTTSTST DDTTDRNGQH
TSGKGALPKT AETTERPAFG FLGVIVVSLM GVLGLKRKQR EE
