ID   B7MHQ7_ECO45            Unreviewed;       586 AA.
AC   B7MHQ7;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   Name=ycbZ {ECO:0000313|EMBL:CAR02308.1};
GN   OrderedLocusNames=ECS88_0976 {ECO:0000313|EMBL:CAR02308.1};
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR02308.1, ECO:0000313|Proteomes:UP000000747};
RN   [1] {ECO:0000313|Proteomes:UP000000747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01122};
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01122}.
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DR   EMBL; CU928161; CAR02308.1; -; Genomic_DNA.
DR   RefSeq; WP_000156501.1; NC_011742.1.
DR   AlphaFoldDB; B7MHQ7; -.
DR   MEROPS; S16.A10; -.
DR   KEGG; ecz:ECS88_0976; -.
DR   HOGENOM; CLU_014785_2_0_6; -.
DR   Proteomes; UP000000747; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10046:SF49; LON PROTEASE HOMOLOG-RELATED; 1.
DR   Pfam; PF13654; AAA_32; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000000747};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          346..543
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        481
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   586 AA;  65864 MW;  FF14E5375321D0F6 CRC64;
     MTITKLAWRD LVPDTDSYQE IFAQPHLIDE NDPLFSDTQP RLQFALEQLL HTRASSSFML
     AKAPEESEYL NLIADAARTL QSDAGQLVGG HYEVSGHTIR LRHAVSADDN FATLTQVVAA
     DWVEAEQLFG CLRQFNGDIT LQPGLVHQAN GGILIISLRT LLAQPLLWMR LKNIVNRERF
     DWVAFDESRP LPVSVPSMPL KLKVILVGER ESLADFQEME PELSEQAIYS EFEDTLQIVD
     AESVSQWCRW VTFTARHNHL PAPGADAWPV LIREAARYTG EQETLPLSPQ WILRQCQEVA
     SLCDGDTFSG EQLNLMLQQR EWREGFLAER MQDEILQEQI LIETEGERIG QINALSVIEF
     PGHPRAFGEP SRISCVVHIG DGEFTDIERK AELGGNIHAK GMMIMQAFLM SELQLEQQIP
     FSASLTFEQS YSEVDGDSAS MAELCALISA LADVPVNQSI AITGSVDQFG RAQPVGGLNE
     KIEGFFAICQ QRELTGKQGV IIPTANVRHL SLHSELVKAV EEDKFTIWAV DDVTDALPLL
     LNLVWDGEGQ TTLMQTIQER IAQASQQEGR HRFPWPLRWL NWFIPN
//