PQQL_ECOLI
ID PQQL_ECOLI Reviewed; 931 AA.
AC P31828; P31829; P76132; P78158;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable zinc protease PqqL;
DE EC=3.4.24.-;
GN Name=pqqL; Synonyms=yddC; OrderedLocusNames=b1494, JW1489;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=9116051; DOI=10.1016/s0300-9084(97)84334-9;
RA Turlin E., Gasser F., Biville F.;
RT "Sequence and functional analysis of an Escherichia coli DNA fragment able
RT to complement pqqE and pqqF mutants from Methylobacterium organophilum.";
RL Biochimie 78:823-831(1996).
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).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA50735.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; X71917; CAA50734.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X71917; CAA50735.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC74567.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15164.2; -; Genomic_DNA.
DR PIR; A64903; A64903.
DR RefSeq; NP_416011.1; NC_000913.3.
DR RefSeq; WP_010723101.1; NZ_CP011343.2.
DR PDB; 6OFS; X-ray; 2.60 A; A=27-931.
DR PDB; 6OFT; X-ray; 2.00 A; A/B=27-497.
DR PDBsum; 6OFS; -.
DR PDBsum; 6OFT; -.
DR AlphaFoldDB; P31828; -.
DR SASBDB; P31828; -.
DR SMR; P31828; -.
DR BioGRID; 4260787; 22.
DR BioGRID; 850420; 1.
DR DIP; DIP-10556N; -.
DR IntAct; P31828; 12.
DR STRING; 511145.b1494; -.
DR MEROPS; M16.A05; -.
DR jPOST; P31828; -.
DR PaxDb; P31828; -.
DR PRIDE; P31828; -.
DR EnsemblBacteria; AAC74567; AAC74567; b1494.
DR EnsemblBacteria; BAA15164; BAA15164; BAA15164.
DR GeneID; 946059; -.
DR KEGG; ecj:JW1489; -.
DR KEGG; eco:b1494; -.
DR PATRIC; fig|511145.12.peg.1561; -.
DR EchoBASE; EB1695; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_008156_0_0_6; -.
DR InParanoid; P31828; -.
DR OMA; RDINAFT; -.
DR PhylomeDB; P31828; -.
DR BioCyc; EcoCyc:EG11744-MON; -.
DR PRO; PR:P31828; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; ISM:EcoCyc.
DR GO; GO:0008233; F:peptidase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; ISM:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; SSF63411; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..931
FT /note="Probable zinc protease PqqL"
FT /id="PRO_0000074415"
FT ACT_SITE 83
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT CONFLICT 360
FT /note="A -> V (in Ref. 1; CAA50734)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="L -> V (in Ref. 1; CAA50735)"
FT /evidence="ECO:0000305"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:6OFT"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:6OFT"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 154..170
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:6OFT"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 297..322
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 328..340
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 343..353
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 357..374
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 378..397
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 404..417
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 424..434
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 440..451
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 456..464
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 465..470
FT /evidence="ECO:0007829|PDB:6OFT"
FT HELIX 474..485
FT /evidence="ECO:0007829|PDB:6OFT"
FT STRAND 511..518
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 521..526
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 543..551
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:6OFS"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 565..573
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 582..591
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 595..600
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 605..612
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 617..628
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 634..649
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 655..667
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 678..683
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 686..694
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 703..709
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 713..723
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 747..757
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 759..768
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 775..796
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 804..813
FT /evidence="ECO:0007829|PDB:6OFS"
FT TURN 814..817
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 818..827
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 832..849
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 853..868
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 869..873
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 874..888
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 893..896
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 897..901
FT /evidence="ECO:0007829|PDB:6OFS"
FT HELIX 906..916
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 917..919
FT /evidence="ECO:0007829|PDB:6OFS"
FT STRAND 921..930
FT /evidence="ECO:0007829|PDB:6OFS"
SQ SEQUENCE 931 AA; 104656 MW; 94A340CA83DB6D1E CRC64;
MEIIMRNLCF LLTLVATLLL PGRLIAAALP QDEKLITGQL DNGLRYMIYP HAHPKDQVNL
WLQIHTGSLQ EEDNELGVAH FVEHMMFNGT KTWPGNKVIE TFESMGLRFG RDVNAYTSYD
ETVYQVSLPT TQKQNLQQVM AIFSEWSNAA TFEKLEVDAE RGVITEEWRA HQDAKWRTSQ
ARRPFLLANT RNLDREPIGL MDTVATVTPA QLRQFYQRWY QPNNMTFIVV GDIDSKEALA
LIKDNLSKLP ANKAAENRVW PTKAENHLRF NIINDKENRV NGIALYYRLP MVQVNDEQSF
IEQAEWSMLV QLFNQRLQER IQSGELKTIS GGTARSVKIA PDYQSLFFRV NARDDNMQDA
ANALMAELAT IDQHGFSAEE LDDVKSTRLT WLKNAVDQQA ERDLRMLTSR LASSSLNNTP
FLSPEETYQL SKRLWQQITV QSLAEKWQQL RKNQDAFWEQ MVNNEVAAKK ALSPAAILAL
EKEYANKKLA AYVFPGRNLS LTVDADPQAE ISSKETLAEN LTSLTLSNGA RVILAKSAGE
EQKLQIIAVS NKGDLSFPAQ QKSLIALANK AVSGSGVGEL SSSSLKRWSA ENSVTMSSKV
SGMNTLLSVS ARTNNPEPGF QLINQRITHS TINDNIWASL QNAQIQALKT LDQRPAEKFA
QQMYETRYAD DRTKLLQENQ IAQFTAADAL AADRQLFSSP ADITFVIVGN VAEDKLVALI
TRYLGSIKHS DSPLAAGKPL TRATDNASVT VKEQNEPVAQ VSQWKRYDSR TPVNLPTRMA
LDAFNVALAK DLRVNIREQA SGAYSVSSRL SVDPQAKDIS HLLAFTCQPE RHDELLTLAN
EVMVKRLAKG ISEQELNEYQ QNVQRSLDIQ QRSVQQLANT IVNSLIQYDD PAAWTEQEQL
LKQMTVENVN TAVKQYLSHP VNTYTGVLLP K
