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Database: UniProt
Entry: E6WCC9_PANSA
LinkDB: E6WCC9_PANSA
Original site: E6WCC9_PANSA 
ID   E6WCC9_PANSA            Unreviewed;       580 AA.
AC   E6WCC9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   OrderedLocusNames=Pat9b_1368 {ECO:0000313|EMBL:ADU68689.1};
OS   Pantoea sp. (strain At-9b).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU68689.1, ECO:0000313|Proteomes:UP000001624};
RN   [1] {ECO:0000313|EMBL:ADU68689.1, ECO:0000313|Proteomes:UP000001624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=At-9b {ECO:0000313|EMBL:ADU68689.1,
RC   ECO:0000313|Proteomes:UP000001624};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT   "Complete sequence chromosome of Pantoea sp. At-9b.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002433; ADU68689.1; -; Genomic_DNA.
DR   RefSeq; WP_013508550.1; NC_014837.1.
DR   AlphaFoldDB; E6WCC9; -.
DR   STRING; 592316.Pat9b_1368; -.
DR   MEROPS; S16.A10; -.
DR   KEGG; pao:Pat9b_1368; -.
DR   eggNOG; COG1067; Bacteria.
DR   HOGENOM; CLU_014785_2_0_6; -.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000001624; 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}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          341..538
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        476
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   580 AA;  64966 MW;  4326E1974EA55E77 CRC64;
     MTSSQLTWQA LQPDSTRYQS IFSNVSLEDS DSLAAVQPRL LNALAHLHHQ QQGFPLLLLR
     SQENSDYLAW VASAAQRFQP DEESLFGGDY LVMGDNVSLL PPAENRPFTS QGGVHYADWI
     EFEQLFGCVR QFKDRVQLEP GLVHRANGGT LILSVNTLLA QPLMWLRLKK CVEQGQFEWH
     SQNERQPLPV AIPPLPLQLR LILCGERDAL ADFQTLDTEA HEMALYSEFE ESLQLVDEDD
     MTSWCQWTLT QAELAGLPAP EADFWPLLIN EAVRNTGDQD TLPLCPRWLR RQMQEAALHG
     DVLNAEALKD ALEARQWRES FLADRMRDEI LLNQIMIETE GEVVGQINGL SVIEFPGHPR
     PWGEPSRITC VVHPGDGEFT DVERKAELGG NIHAKGMMIM QAYLIAELEL EQQLPFSASL
     VFEQSYSEVD GDSASLAELC ALISALANQP LNQQIAVTGS VDQFGNVQPV GGLNEKIEGF
     FSICNERGLT GQQGVILPAS NVRHLSLNAA VVEAVQQGQF HIWAIESVDE ALPLLTGVAW
     QSESGDSLLS TIQERIAQLN QQETRQRPWP LRWLNWFNHS
//
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