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YCAL_ECOLI
ID   YCAL_ECOLI              Reviewed;         254 AA.
AC   P43674; P75840;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 3.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Metalloprotease YcaL {ECO:0000305};
DE            EC=3.4.-.- {ECO:0000269|PubMed:28784813};
DE   Flags: Precursor;
GN   Name=ycaL; OrderedLocusNames=b0909, JW0892;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-183.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Palma C.A., Allen E., Araujo R., Aparicio A.M., Botstein D., Cherry M.,
RA   Chung E., Dietrich F., Duncan M., Federspiel N., Kalman S., Kim K.,
RA   Komp C., Lashkari D., Lew H., Lin D., Namath A., Oefner P., Davis R.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-254.
RC   STRAIN=K12;
RX   PubMed=7836281; DOI=10.1128/jb.177.3.517-523.1995;
RA   Fricke J., Neuhard J., Kelln R.A., Pedersen S.;
RT   "The cmk gene encoding cytidine monophosphate kinase is located in the rpsA
RT   operon and is required for normal replication rate in Escherichia coli.";
RL   J. Bacteriol. 177:517-523(1995).
RN   [6]
RP   FUNCTION AS A PROTEASE.
RX   PubMed=28784813; DOI=10.1128/jb.00418-17;
RA   Soltes G.R., Martin N.R., Park E., Sutterlin H.A., Silhavy T.J.;
RT   "Distinctive roles for periplasmic proteases in the maintenance of
RT   essential outer membrane protein assembly.";
RL   J. Bacteriol. 199:E00418-E00418(2017).
CC   -!- FUNCTION: Involved in the degradation of the LPS-assembly protein LptD.
CC       Degrades LptD that have engaged the Bam complex but are stalled at an
CC       early step in the outer membrane protein assembly process.
CC       {ECO:0000269|PubMed:28784813}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O75844};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75844};
CC   -!- INTERACTION:
CC       P43674; P0AAM7: hybG; NbExp=2; IntAct=EBI-9128400, EBI-562426;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- MISCELLANEOUS: YcaL, BepA and DegP degrade stalled LptD substrate at
CC       distinct points in the outer membrane protein assembly.
CC       {ECO:0000269|PubMed:28784813}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA81515.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U00096; AAC73995.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35644.1; -; Genomic_DNA.
DR   EMBL; U31523; AAA81515.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X82933; CAA58106.1; -; Genomic_DNA.
DR   PIR; D64830; D64830.
DR   RefSeq; NP_415429.2; NC_000913.3.
DR   RefSeq; WP_001350496.1; NZ_LN832404.1.
DR   AlphaFoldDB; P43674; -.
DR   SMR; P43674; -.
DR   BioGRID; 4260012; 9.
DR   BioGRID; 849908; 2.
DR   DIP; DIP-11467N; -.
DR   IntAct; P43674; 2.
DR   STRING; 511145.b0909; -.
DR   MEROPS; M48.A03; -.
DR   PaxDb; P43674; -.
DR   PRIDE; P43674; -.
DR   EnsemblBacteria; AAC73995; AAC73995; b0909.
DR   EnsemblBacteria; BAA35644; BAA35644; BAA35644.
DR   GeneID; 945534; -.
DR   KEGG; ecj:JW0892; -.
DR   KEGG; eco:b0909; -.
DR   PATRIC; fig|1411691.4.peg.1367; -.
DR   EchoBASE; EB2932; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_074068_0_0_6; -.
DR   InParanoid; P43674; -.
DR   OMA; RPNIPYT; -.
DR   PhylomeDB; P43674; -.
DR   BioCyc; EcoCyc:G6470-MON; -.
DR   PRO; PR:P43674; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; TAS:EcoCyc.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR001915; Peptidase_M48.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Hydrolase; Lipoprotein; Membrane;
KW   Metal-binding; Metalloprotease; Palmitate; Protease; Reference proteome;
KW   Signal; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..254
FT                   /note="Metalloprotease YcaL"
FT                   /id="PRO_0000138937"
FT   REGION          227..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000250|UniProtKB:O75844"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O75844"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O75844"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O75844"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CONFLICT        241..254
FT                   /note="ERAQHIRDRIASGK -> DVRNTSVIVSPLVSKSLSSLRWSSASPL (in
FT                   Ref. 5; CAA58106)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   254 AA;  26740 MW;  4DDF70D17E9D93A0 CRC64;
     MKNTKLLLAI ATSAALLTGC QNTHGIDTNM AISSGLNAYK AATLSDADAK AIANQGCAEM
     DSGNQVASKS SKYGKRLAKI AKALGNNING TPVNYKVYMT SDVNAWAMAN GCVRVYSGLM
     DMMNDNEIEG VLGHELGHVA LGHSLAEMKA SYAIVAARDA ISATSGVASQ LSRSQLGDIA
     EGAINAKYSR DKESEADDFS FDLLKKRGIS TQGLVGSFET LASLDGGRTQ SMFDSHPPST
     ERAQHIRDRI ASGK
 
 
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