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LONH_ECOLI
ID   LONH_ECOLI              Reviewed;         586 AA.
AC   P75867;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Putative Lon protease homolog;
DE            EC=3.4.21.-;
DE   AltName: Full=ATP-dependent protease La homolog;
GN   Name=ycbZ; OrderedLocusNames=b0955, JW0938;
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).
CC   -!- DOMAIN: Lacks the ATP-binding domain.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01122}.
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DR   EMBL; U00096; AAC74041.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35713.1; -; Genomic_DNA.
DR   PIR; B64836; B64836.
DR   RefSeq; NP_415475.1; NC_000913.3.
DR   RefSeq; WP_000156518.1; NZ_LN832404.1.
DR   AlphaFoldDB; P75867; -.
DR   SMR; P75867; -.
DR   BioGRID; 4260030; 40.
DR   DIP; DIP-11487N; -.
DR   STRING; 511145.b0955; -.
DR   MEROPS; S16.A10; -.
DR   jPOST; P75867; -.
DR   PaxDb; P75867; -.
DR   PRIDE; P75867; -.
DR   EnsemblBacteria; AAC74041; AAC74041; b0955.
DR   EnsemblBacteria; BAA35713; BAA35713; BAA35713.
DR   GeneID; 945569; -.
DR   KEGG; ecj:JW0938; -.
DR   KEGG; eco:b0955; -.
DR   PATRIC; fig|1411691.4.peg.1319; -.
DR   EchoBASE; EB3482; -.
DR   eggNOG; COG1067; Bacteria.
DR   InParanoid; P75867; -.
DR   OMA; GFFTICQ; -.
DR   PhylomeDB; P75867; -.
DR   BioCyc; EcoCyc:G6493-MON; -.
DR   PRO; PR:P75867; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR041699; AAA_32.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; PTHR10046; 1.
DR   Pfam; PF13654; AAA_32; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Serine protease.
FT   CHAIN           1..586
FT                   /note="Putative Lon protease homolog"
FT                   /id="PRO_0000076148"
FT   DOMAIN          346..543
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        481
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   586 AA;  65819 MW;  442AAEADDB87B59F CRC64;
     MTITKLAWRD LVPDTDSYQE IFAQPHLIDE NDPLFSDTQP RLQFALEQLL HTRASSSFML
     AKAPEESEYL NLIANAARTL QSDAGQLVGG HYEVSGHSIR LRHAVSADDN FATLTQVVAA
     DWVEAEQLFG CLRQFNGDIT LQPGLVHQAN GGILIISLRT LLAQPLLWMR LKNIVNRERF
     DWVAFDESRP LPVSVPSMPL KLKVILVGER ESLADFQEME PELSEQAIYS EFEDTLQIVD
     AESVTQWCRW VTFTARHNHL PAPGADAWPI LIREAARYTG EQETLPLSPQ WILRQCKEVA
     SLCDGDTFSG EQLNLMLQQR EWREGFLAER MQDEILQEQI LIETEGERIG QINALSVIEF
     PGHPRAFGEP SRISCVVHIG DGEFTDIERK AELGGNIHAK GMMIMQAFLM SELQLEQQIP
     FSASLTFEQS YSEVDGDSAS MAELCALISA LADVPVNQSI AITGSVDQFG RAQPVGGLNE
     KIEGFFAICQ QRELTGKQGV IIPTANVRHL SLHSELVKAV EEGKFTIWAV DDVTDALPLL
     LNLVWDGEGQ TTLMQTIQER IAQASQQEGR HRFPWPLRWL NWFIPN
 
 
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