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 24-JAN-2024, entry version 145.
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; Pseudomonadota; 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; 511145-b0909; -.
DR EnsemblBacteria; AAC73995; AAC73995; b0909.
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 OrthoDB; 9810445at2; -.
DR PhylomeDB; P43674; -.
DR BioCyc; EcoCyc:G6470-MONOMER; -.
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 CDD; cd07334; M48C_loiP_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF8; METALLOPROTEASE YCAL; 1.
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
//
