P3P_LACLS
ID P3P_LACLS Reviewed; 1962 AA.
AC P15292; Q02VE4;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=PIII-type proteinase;
DE EC=3.4.21.96;
DE AltName: Full=Cell wall-associated serine proteinase;
DE AltName: Full=Lactocepin;
DE Flags: Precursor;
GN Name=prtP; OrderedLocusNames=LACR_C42;
OS Lactococcus lactis subsp. cremoris (strain SK11).
OG Plasmid pSK111, and Plasmid pLACR3.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=272622;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 188-197.
RC PLASMID=pSK111;
RX PubMed=2760036; DOI=10.1016/s0021-9258(18)80036-9;
RA Vos P., Simons G., Siezen R.J., de Vos W.M.;
RT "Primary structure and organization of the gene for a procaryotic, cell
RT envelope-located serine proteinase.";
RL J. Biol. Chem. 264:13579-13585(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK11; PLASMID=pLACR3;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; J04962; AAA03533.1; ALT_SEQ; Unassigned_DNA.
DR EMBL; CP000428; ABJ74078.1; -; Genomic_DNA.
DR RefSeq; WP_011669079.1; NC_008505.1.
DR AlphaFoldDB; P15292; -.
DR SMR; P15292; -.
DR MEROPS; S08.019; -.
DR MEROPS; S08.116; -.
DR EnsemblBacteria; ABJ74078; ABJ74078; LACR_C42.
DR KEGG; llc:LACR_C42; -.
DR HOGENOM; CLU_001299_0_0_9; -.
DR OMA; KNSAMNT; -.
DR SABIO-RK; P15292; -.
DR Proteomes; UP000000240; Plasmid pLACR3.
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 Plasmid; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..33
FT PROPEP 34..187
FT /evidence="ECO:0000269|PubMed:2760036"
FT /id="PRO_0000027095"
FT CHAIN 188..1930
FT /note="PIII-type proteinase"
FT /id="PRO_0000027096"
FT PROPEP 1931..1962
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000027097"
FT DOMAIN 191..697
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 1796..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1927..1931
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 1828..1869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1890..1928
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 1930
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 109
FT /note="T -> I (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="A -> V (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="T -> K (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="T -> S (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="T -> K (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="L -> V (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="D -> N (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="E -> D (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1213
FT /note="T -> M (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1251
FT /note="D -> H (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1282
FT /note="E -> K (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1304
FT /note="N -> K (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1313
FT /note="T -> K (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1316..1318
FT /note="ANE -> TNK (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1394
FT /note="T -> S (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1448
FT /note="V -> E (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1515
FT /note="K -> Q (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1523
FT /note="S -> A (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1550
FT /note="V -> I (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1673
FT /note="A -> D (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1685
FT /note="S -> P (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1719
FT /note="V -> I (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1722
FT /note="A -> E (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1859..1918
FT /note="Missing (in Ref. 1; AAA03533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1962 AA; 205996 MW; 39B5FD18598DC5CC 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 LQDNEMVGSP GTSRGATTVA
SAENTDVITQ AVTITDGTGL QLGPETIQLS SHDFTGSFDQ KKFYIVKDAS GNLSKGALAD
YTADAKGKIA IVKRGEFSFD DKQKYAQAAG AAGLIIVNTD GTATPMTSIA LTTTFPTFGL
SSVTGQKLVD WVTAHPDDSL GVKITLAMLP 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 GNFGTVPLLK NKNTGTQYYG GMVTDADGNK TVDDQAIAFS SDKNALYNEI
SMKYYLLRNI SNVQVDILDG QGNKVTTLSS STNRKKTYYN AHSQQYIYYN APAWDGTYYD
QRDGNIKTAD DGSYTYRISG VPEGGDKRQV FDVPFKLDSK APTVRHVALS AKTENGKTQY
YLTAEAKDDL SGLDATKSVK TEINEVTNLD 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 DAPVYTNDPN 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 VKAALGTDLG
NQTDSSTGKT FTAALDDLVA QAQAGTQTDD QLQATLAKVL DAVLAKLAEG IKAATPAEVG
NAKDAATGKT WYADIADTLT SGQASADASD KLAHLQALQS LKTKVAAAVE AAKTVGKGDG
TTGTSDKGGG QGTPAPAPGD TGKDKGDEGS QPSSGGNIPT KPATTTSTTT DDTTDRNGQL
TSGTSDKGGG QGTPAPAPGD IGKDKGDEGS QPSSGGNIPT NPATTTSTTT DDTTDRNGQL
TSGKGALPKT GETTERPAFG FLGVIVVSLM GVLGLKRKQR EE
