ID   B8CPF1_SHEPW            Unreviewed;       567 AA.
AC   B8CPF1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   OrderedLocusNames=swp_2801 {ECO:0000313|EMBL:ACJ29527.1};
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849 {ECO:0000313|EMBL:ACJ29527.1, ECO:0000313|Proteomes:UP000000753};
RN   [1] {ECO:0000313|EMBL:ACJ29527.1, ECO:0000313|Proteomes:UP000000753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877 {ECO:0000313|Proteomes:UP000000753};
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ29527.1; -; Genomic_DNA.
DR   RefSeq; WP_020912881.1; NC_011566.1.
DR   AlphaFoldDB; B8CPF1; -.
DR   STRING; 225849.swp_2801; -.
DR   MEROPS; S16.A10; -.
DR   KEGG; swp:swp_2801; -.
DR   eggNOG; COG1067; Bacteria.
DR   HOGENOM; CLU_014785_2_0_6; -.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000000753; 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; IPR046843; LonB_AAA-LID.
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   Pfam; PF20436; LonB_AAA-LID; 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          323..518
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        413
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        456
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   567 AA;  63504 MW;  301E3A09AE2445EC CRC64;
     MNSNIIPASA LKPQFTLTTA AADNSPSEVR LIGQSRVRDA FKLLSNTHDQ HMYLADYSGC
     NRKNIIRALV ETEGVFVDKN LVLTGNGTAW CEQSDKQQLL AAKQTTHQYL SGTIKKHDLI
     GRYDERTKHY RAGALANCHY LFICADSIWK RETLWELLLE ILDKKEYQVH SSLPPIALNC
     KIILIGSSNQ YGHCWLGEPI FANLFPLLGE LLNEVDLNEV PLAHYNQWLD CILEDISLTI
     DDPARLALLE YSARLADHQQ RLSLMSINIE QLLVQASTYS QQTHIDEKAF RLSIDMFNQR
     HNASEKLSEQ NFDDLFINLP TQDEIIGQIN GLTVIENAEY SYGEPARITA SVHYGDGEVA
     DIERKSELGG NIHAKGMMIL SSCLYRIFGK DAPLHLNANI VFEQSYQEID GDSASLAEYC
     SLISAISEKP IKQSIAATGA IDQFGNVQAI GGVNEKIEGF FKLCQRRGLT GHQGVIIPCS
     NMQQLNLHQS VINAVNEGQF TLYQVKHIDE AAEILMQTPA GTADQDNQFP NDSLYGLVQT
     RLEGLAGYQE EEKSFFVRLR EKLSFSS
//