LOIP_ECOLI
ID LOIP_ECOLI Reviewed; 252 AA.
AC P25894; P76646; Q2M9Q7;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Metalloprotease LoiP;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=loiP; Synonyms=yggG; OrderedLocusNames=b2936, JW2903;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2153656; DOI=10.1128/jb.172.2.538-547.1990;
RA Szumanski M.B.W., Boyle S.M.;
RT "Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a
RT putrescine biosynthetic enzyme in Escherichia coli.";
RL J. Bacteriol. 172:538-547(1990).
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 FUNCTION.
RX PubMed=1310091; DOI=10.1128/jb.174.3.758-764.1992;
RA Szumanski M.B.W., Boyle S.M.;
RT "Influence of cyclic AMP, agmatine, and a novel protein encoded by a
RT flanking gene on speB (agmatine ureohydrolase) in Escherichia coli.";
RL J. Bacteriol. 174:758-764(1992).
RN [5]
RP FUNCTION, INTERACTION WITH ERA, AND INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17651431; DOI=10.1111/j.1574-6968.2007.00860.x;
RA Huang Y., Zhang B., Dong K., Zhang X., Hou L., Wang T., Chen N., Chen S.;
RT "Up-regulation of yggG promotes the survival of Escherichia coli cells
RT containing Era-1 mutant protein.";
RL FEMS Microbiol. Lett. 275:8-15(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17909889; DOI=10.1007/s00284-007-9030-7;
RA Huang Y., Dong K., Zhang X., Zhang B., Hou L., Chen N., Chen S.;
RT "Expression and regulation of the yggG gene of Escherichia coli.";
RL Curr. Microbiol. 56:14-20(2008).
RN [7]
RP FUNCTION AS A PROTEASE, INTERACTION WITH BEPA, SUBCELLULAR LOCATION,
RP INDUCTION, DISULFIDE BOND, AND GENE NAME.
RX PubMed=22491786; DOI=10.1039/c2mb05506f;
RA Lutticke C., Hauske P., Lewandrowski U., Sickmann A., Kaiser M.,
RA Ehrmann M.;
RT "E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.";
RL Mol. Biosyst. 8:1775-1782(2012).
CC -!- FUNCTION: Metalloprotease that cleaves substrates preferentially
CC between Phe-Phe residues. Plays a role in response to some stress
CC conditions. Seems to regulate the expression of speB.
CC {ECO:0000269|PubMed:1310091, ECO:0000269|PubMed:17651431,
CC ECO:0000269|PubMed:17909889, ECO:0000269|PubMed:22491786}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Interacts with Era and BepA. {ECO:0000269|PubMed:17651431,
CC ECO:0000269|PubMed:22491786}.
CC -!- INTERACTION:
CC P25894; P0A6D5: ydiB; NbExp=2; IntAct=EBI-560654, EBI-560638;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:17909889,
CC ECO:0000269|PubMed:22491786}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:17909889,
CC ECO:0000269|PubMed:22491786}. Note=Proper membrane localization can
CC depend on BepA.
CC -!- INDUCTION: Induced by heat shock and low osmolarity.
CC {ECO:0000269|PubMed:17651431, ECO:0000269|PubMed:17909889,
CC ECO:0000269|PubMed:22491786}.
CC -!- PTM: The intramolecular disulfide bond improves the stability and the
CC activity of LoiP. It forms even in the absence of the oxido-reductase
CC DsbA (PubMed:22491786). {ECO:0000269|PubMed:22491786}.
CC -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69103.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA83911.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M32363; AAA83911.1; ALT_INIT; Genomic_DNA.
DR EMBL; U28377; AAA69103.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75973.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76999.1; -; Genomic_DNA.
DR PIR; G65078; G65078.
DR RefSeq; NP_417411.2; NC_000913.3.
DR RefSeq; WP_001326497.1; NZ_LN832404.1.
DR AlphaFoldDB; P25894; -.
DR SMR; P25894; -.
DR BioGRID; 4263066; 14.
DR DIP; DIP-12186N; -.
DR IntAct; P25894; 3.
DR STRING; 511145.b2936; -.
DR MEROPS; M48.022; -.
DR jPOST; P25894; -.
DR PaxDb; P25894; -.
DR PRIDE; P25894; -.
DR EnsemblBacteria; AAC75973; AAC75973; b2936.
DR EnsemblBacteria; BAE76999; BAE76999; BAE76999.
DR GeneID; 945173; -.
DR KEGG; ecj:JW2903; -.
DR KEGG; eco:b2936; -.
DR PATRIC; fig|1411691.4.peg.3797; -.
DR EchoBASE; EB1268; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_074068_0_0_6; -.
DR InParanoid; P25894; -.
DR OMA; LNYKVYL; -.
DR PhylomeDB; P25894; -.
DR BioCyc; EcoCyc:EG11291-MON; -.
DR BioCyc; MetaCyc:EG11291-MON; -.
DR PRO; PR:P25894; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; IDA:EcoCyc.
DR GO; GO:0071476; P:cellular hypotonic response; IEP:EcoCyc.
DR GO; GO:0034605; P:cellular response to heat; IEP:EcoCyc.
DR GO; GO:0034644; P:cellular response to UV; IEP: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 outer membrane; Disulfide bond; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Metalloprotease; Palmitate; Protease; Reference proteome;
KW Signal; Stress response; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..252
FT /note="Metalloprotease LoiP"
FT /id="PRO_0000138938"
FT REGION 224..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT DISULFID 53..108
FT /evidence="ECO:0000269|PubMed:22491786"
SQ SEQUENCE 252 AA; 26842 MW; E4C4718073B5C5B6 CRC64;
MKIRALLVAM SVATVLTGCQ NMDSNGLLSS GAEAFQAYSL SDAQVKTLSD QACQEMDSKA
TIAPANSEYA KRLTTIANAL GNNINGQPVN YKVYMAKDVN AFAMANGCIR VYSGLMDMMT
DNEVEAVIGH EMGHVALGHV KKGMQVALGT NAVRVAAASA GGIVGSLSQS QLGNLGEKLV
NSQFSQRQEA EADDYSYDLL RQRGISPAGL ATSFEKLAKL EEGRQSSMFD DHPASAERAQ
HIRDRMSADG IK
