ID A0KKK1_AERHH Unreviewed; 659 AA.
AC A0KKK1;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 08-NOV-2023, entry version 84.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=AHA_2279 {ECO:0000313|EMBL:ABK39614.1};
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39614.1, ECO:0000313|Proteomes:UP000000756};
RN [1] {ECO:0000313|EMBL:ABK39614.1, ECO:0000313|Proteomes:UP000000756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC KCTC 2358 / NCIMB 9240 / NCTC 8049
RC {ECO:0000313|Proteomes:UP000000756};
RX PubMed=16980456; DOI=10.1128/JB.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK39614.1; -; Genomic_DNA.
DR RefSeq; WP_011706132.1; NC_008570.1.
DR RefSeq; YP_856802.1; NC_008570.1.
DR AlphaFoldDB; A0KKK1; -.
DR STRING; 380703.AHA_2279; -.
DR MEROPS; S16.A10; -.
DR EnsemblBacteria; ABK39614; ABK39614; AHA_2279.
DR KEGG; aha:AHA_2279; -.
DR PATRIC; fig|380703.7.peg.2279; -.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_014785_0_1_6; -.
DR OMA; GFFTICQ; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000000756; 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; 1.10.8.60; -; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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 ECO:0000313|EMBL:ABK39614.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 419..616
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 554
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 659 AA; 73367 MW; EA81EB202F9E44ED CRC64;
MAELTSEQLK PVFSIEQFPA LSELEPIPFA ALQPRAISAI KRLASFDGDC PVMLLNGFPG
VDYEGVCQTL IAASNGKDGD LFDLCYTENL NNPFKPIWLR LQPGTGFEFC EMVGELLKLM
SHHLDAERLV TRIMRKQNND PKIDDFLSDL AAHVAQGLEF QHPVLINLLI HHEEQAAPVI
YGRDLNWDTL FGSINYQTEQ GSVYANQHLL EPGLLRQANG GYLILQLDEL LDQPHLWFKL
KNAMQKGELD WNAYQEGKTL TPFFTPEATP IKLKLILVGD RLDVAEFQML DRDMSERIFL
RADLVSEVNI EEDLPDYLQY LAWLRERWEL LDFTPAALAA LCRHASRLCD HQEWLSLSEV
QLSAIMRMAD SLARELEADV VTDEHIRGAL EEQDYRLNYL VEQSDQGVID GQILLQTDGE
EVGQINGLSV IQVSGHPYDF GEPVRLTATV HLGDGDVADI ERKAELAGHI HAKAMMIIHG
YLSNKFGAEN PSPLSANLVF EQSYHEIDGD SASLTGLCAL LSALARQPIY QHFAVTGAVD
QFGNVQAVGG VNEKIEGFFR VCKIHGLTGK QGILLPGTNA QQLNLSDEVI AAVEAGQFHI
HPVDHVEEAI ELLTGCVAGE PDMPDTLFGR IQQRLDELNG TDVIKGGVLR RLLGRVFGR
//