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
//