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SPPA_ECOLI
ID   SPPA_ECOLI              Reviewed;         618 AA.
AC   P08395; P77752; Q46723; Q46724; Q46725; Q46726; Q57183;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Protease 4;
DE            EC=3.4.21.-;
DE   AltName: Full=Endopeptidase IV;
DE   AltName: Full=Protease IV;
DE   AltName: Full=Signal peptide peptidase;
GN   Name=sppA; OrderedLocusNames=b1766, JW1755;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, SUBUNIT,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=K12 / CS520;
RX   PubMed=3522590; DOI=10.1016/s0021-9258(18)67669-0;
RA   Ichihara S., Suzuki T., Suzuki M., Mizushima S.;
RT   "Molecular cloning and sequencing of the sppA gene and characterization of
RT   the encoded protease IV, a signal peptide peptidase, of Escherichia coli.";
RL   J. Biol. Chem. 261:9405-9411(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-433.
RC   STRAIN=Various ECOR strains;
RX   PubMed=7973728; DOI=10.1126/science.7973728;
RA   Guttman D.S., Dykhuizen D.E.;
RT   "Clonal divergence in Escherichia coli as a result of recombination, not
RT   mutation.";
RL   Science 266:1380-1383(1994).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, ACTIVE SITE, TOPOLOGY, AND MUTAGENESIS OF
RP   LYS-209; LYS-366; SER-409; GLY-410; TYR-412; HIS-510 AND ASP-524.
RC   STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX   PubMed=18476724; DOI=10.1021/bi800657p;
RA   Wang P., Shim E., Cravatt B., Jacobsen R., Schoeniger J., Kim A.C.,
RA   Paetzel M., Dalbey R.E.;
RT   "Escherichia coli signal peptide peptidase A is a serine-lysine protease
RT   with a lysine recruited to the nonconserved amino-terminal domain in the
RT   S49 protease family.";
RL   Biochemistry 47:6361-6369(2008).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=21810987; DOI=10.1073/pnas.1108376108;
RA   Saito A., Hizukuri Y., Matsuo E., Chiba S., Mori H., Nishimura O., Ito K.,
RA   Akiyama Y.;
RT   "Post-liberation cleavage of signal peptides is catalyzed by the site-2
RT   protease (S2P) in bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13740-13745(2011).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 47-618, FUNCTION, ACTIVE SITE,
RP   TOPOLOGY, AND SUBUNIT.
RC   STRAIN=K12;
RX   PubMed=18164727; DOI=10.1016/j.jmb.2007.11.080;
RA   Kim A.C., Oliver D.C., Paetzel M.;
RT   "Crystal structure of a bacterial signal peptide peptidase.";
RL   J. Mol. Biol. 376:352-366(2008).
CC   -!- FUNCTION: Digests cleaved signal peptides in vitro, its in vivo
CC       function is unknown. This activity is necessary to maintain proper
CC       secretion of mature proteins across the membrane.
CC       {ECO:0000269|PubMed:18164727, ECO:0000269|PubMed:18476724,
CC       ECO:0000269|PubMed:21810987, ECO:0000269|PubMed:3522590}.
CC   -!- ACTIVITY REGULATION: Inhibited by serine hydrolase inhibitor FP-biotin
CC       and by antipain. {ECO:0000269|PubMed:3522590}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18164727,
CC       ECO:0000269|PubMed:3522590}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:18476724,
CC       ECO:0000269|PubMed:3522590}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:18476724, ECO:0000269|PubMed:3522590}.
CC   -!- DOMAIN: A tandem duplication in the protein fold creates an intact
CC       active site between the repeated domains of each monomer.
CC   -!- DISRUPTION PHENOTYPE: No effect on processing of liberated signal
CC       peptides in vivo. {ECO:0000269|PubMed:21810987}.
CC   -!- SIMILARITY: Belongs to the peptidase S49 family. {ECO:0000305}.
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DR   EMBL; M13359; AAA24648.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74836.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15557.1; -; Genomic_DNA.
DR   EMBL; U13772; AAA57008.1; -; Genomic_DNA.
DR   EMBL; U13773; AAA57009.1; -; Genomic_DNA.
DR   EMBL; U13774; AAA57010.1; -; Genomic_DNA.
DR   EMBL; U13775; AAA57011.1; -; Genomic_DNA.
DR   EMBL; U13776; AAA57012.1; -; Genomic_DNA.
DR   EMBL; U13777; AAA57013.1; -; Genomic_DNA.
DR   EMBL; U13778; AAA57014.1; -; Genomic_DNA.
DR   EMBL; U13779; AAA57015.1; -; Genomic_DNA.
DR   EMBL; U13780; AAA57016.1; -; Genomic_DNA.
DR   EMBL; U13782; AAA57017.1; -; Genomic_DNA.
DR   EMBL; U13833; AAA57030.1; -; Genomic_DNA.
DR   EMBL; U13834; AAA57031.1; -; Genomic_DNA.
DR   PIR; F64936; PRECT4.
DR   PIR; I81191; I81191.
DR   RefSeq; NP_416280.1; NC_000913.3.
DR   RefSeq; WP_001259810.1; NZ_SSZK01000001.1.
DR   PDB; 3BEZ; X-ray; 2.76 A; A/B/C/D=47-618.
DR   PDB; 3BF0; X-ray; 2.55 A; A/B/C/D=47-618.
DR   PDBsum; 3BEZ; -.
DR   PDBsum; 3BF0; -.
DR   AlphaFoldDB; P08395; -.
DR   SMR; P08395; -.
DR   BioGRID; 4259140; 22.
DR   IntAct; P08395; 1.
DR   STRING; 511145.b1766; -.
DR   MEROPS; S49.001; -.
DR   jPOST; P08395; -.
DR   PaxDb; P08395; -.
DR   PRIDE; P08395; -.
DR   EnsemblBacteria; AAC74836; AAC74836; b1766.
DR   EnsemblBacteria; BAA15557; BAA15557; BAA15557.
DR   GeneID; 946281; -.
DR   KEGG; ecj:JW1755; -.
DR   KEGG; eco:b1766; -.
DR   PATRIC; fig|1411691.4.peg.488; -.
DR   EchoBASE; EB0961; -.
DR   eggNOG; COG0616; Bacteria.
DR   HOGENOM; CLU_008856_1_1_6; -.
DR   InParanoid; P08395; -.
DR   OMA; DPKGQYL; -.
DR   PhylomeDB; P08395; -.
DR   BioCyc; EcoCyc:EG10968-MON; -.
DR   BioCyc; MetaCyc:EG10968-MON; -.
DR   EvolutionaryTrace; P08395; -.
DR   PRO; PR:P08395; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:EcoCyc.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006465; P:signal peptide processing; IMP:EcoliWiki.
DR   CDD; cd07019; S49_SppA_1; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR004634; Pept_S49_pIV.
DR   InterPro; IPR004635; Pept_S49_SppA.
DR   InterPro; IPR002142; Peptidase_S49.
DR   InterPro; IPR033854; S49_SppA_1.
DR   Pfam; PF01343; Peptidase_S49; 2.
DR   PIRSF; PIRSF001217; Protease_4_SppA; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   TIGRFAMs; TIGR00705; SppA_67K; 1.
DR   TIGRFAMs; TIGR00706; SppA_dom; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Protease; Reference proteome; Serine protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..618
FT                   /note="Protease 4"
FT                   /id="PRO_0000171438"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT   TOPO_DOM        46..618
FT                   /note="Periplasmic"
FT   ACT_SITE        209
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        409
FT                   /note="Nucleophile"
FT   VARIANT         151
FT                   /note="V -> I (in strain: ECOR 49 and ECOR 50)"
FT   VARIANT         186
FT                   /note="G -> S (in strain: ECOR 16)"
FT   VARIANT         252
FT                   /note="E -> H (in strain: ECOR 16)"
FT   VARIANT         252
FT                   /note="E -> K (in strain: ECOR 49)"
FT   VARIANT         252
FT                   /note="E -> Q (in strain: ECOR 38, ECOR 39, ECOR 40, ECOR
FT                   50, ECOR 65 and ECOR 68)"
FT   VARIANT         294
FT                   /note="A -> T (in strain: ECOR 38, ECOR 39, ECOR 40, ECOR
FT                   49, ECOR 50 and ECOR 65)"
FT   MUTAGEN         209
FT                   /note="K->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:18476724"
FT   MUTAGEN         366
FT                   /note="K->A: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:18476724"
FT   MUTAGEN         409
FT                   /note="S->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:18476724"
FT   MUTAGEN         410
FT                   /note="G->A: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:18476724"
FT   MUTAGEN         412
FT                   /note="Y->F: No effect on activity."
FT                   /evidence="ECO:0000269|PubMed:18476724"
FT   MUTAGEN         510
FT                   /note="H->A: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:18476724"
FT   MUTAGEN         524
FT                   /note="D->N: Increased activity."
FT                   /evidence="ECO:0000269|PubMed:18476724"
FT   CONFLICT        378
FT                   /note="S -> T (in Ref. 1; AAA24648 and 5; AAA57009)"
FT                   /evidence="ECO:0000305"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           97..109
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          122..125
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           128..143
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           157..163
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          166..171
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           190..195
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          199..205
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           213..216
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           222..247
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           251..254
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           257..266
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   TURN            267..270
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           272..278
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          281..285
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           288..299
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   TURN            303..305
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          306..312
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   TURN            313..315
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          327..342
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          346..348
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           349..361
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          365..377
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           379..394
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          399..408
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           410..413
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   TURN            414..417
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          419..423
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          428..430
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          434..440
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           442..447
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          451..453
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           459..461
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           471..495
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           500..504
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          511..513
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           514..519
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          524..526
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   HELIX           529..539
FT                   /evidence="ECO:0007829|PDB:3BF0"
FT   STRAND          545..548
FT                   /evidence="ECO:0007829|PDB:3BF0"
SQ   SEQUENCE   618 AA;  67219 MW;  EAF00496B5946AC3 CRC64;
     MRTLWRFIAG FFKWTWRLLN FVREMVLNLF FIFLVLVGVG IWMQVSGGDS KETASRGALL
     LDISGVIVDK PDSSQRFSKL SRQLLGASSD RLQENSLFDI VNTIRQAKDD RNITGIVMDL
     KNFAGGDQPS MQYIGKALKE FRDSGKPVYA VGENYSQGQY YLASFANKIW LSPQGVVDLH
     GFATNGLYYK SLLDKLKVST HVFRVGTYKS AVEPFIRDDM SPAAREADSR WIGELWQNYL
     NTVAANRQIP AEQVFPGAQG LLEGLTKTGG DTAKYALENK LVDALASSAE IEKALTKEFG
     WSKTDKNYRA ISYYDYALKT PADTGDSIGV VFANGAIMDG EETQGNVGGD TTAAQIRDAR
     LDPKVKAIVL RVNSPGGSVT ASEVIRAELA AARAAGKPVV VSMGGMAASG GYWISTPANY
     IVANPSTLTG SIGIFGVITT VENSLDSIGV HTDGVSTSPL ADVSITRALP PEAQLMMQLS
     IENGYKRFIT LVADARHSTP EQIDKIAQGH VWTGQDAKAN GLVDSLGDFD DAVAKAAELA
     KVKQWHLEYY VDEPTFFDKV MDNMSGSVRA MLPDAFQAML PAPLASVAST VKSESDKLAA
     FNDPQNRYAF CLTCANMR
 
 
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