ID A8AIC4_CITK8 Unreviewed; 586 AA.
AC A8AIC4;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=CKO_02113 {ECO:0000313|EMBL:ABV13237.1};
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV13237.1, ECO:0000313|Proteomes:UP000008148};
RN [1] {ECO:0000313|EMBL:ABV13237.1, ECO:0000313|Proteomes:UP000008148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC {ECO:0000313|Proteomes:UP000008148};
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) 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; CP000822; ABV13237.1; -; Genomic_DNA.
DR RefSeq; WP_012132969.1; NC_009792.1.
DR AlphaFoldDB; A8AIC4; -.
DR STRING; 290338.CKO_02113; -.
DR MEROPS; S16.A10; -.
DR GeneID; 45136060; -.
DR KEGG; cko:CKO_02113; -.
DR HOGENOM; CLU_014785_2_0_6; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000008148; 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:UP000008148};
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; 65840 MW; BEE6C4A0A9630983 CRC64;
MTITKLAWRD LVPDTDSYQE IFAQPHFTDE SATLLSDTQP RLQFALEQLL QPWASSSFML
AKAPEEPEYL TLLSDAARTL QADAGQLTGG HYEISGHTIR YRAAEKAEDN FATSAQVVSA
DWVEAEQLFG CLRQFNGEIT LQPGLVHQAN GGVLVISLRT LLAQPLLWMR LKAIVSHNRF
DWVAFDESRP LPVSVPSMPL KLKVVLVGER ESLADFQEME PELAEQAIYS EFEDNLQIVD
AETMTQWCQW VQHTLKRNNL PTPTPDAWQV LVREAVRYTG EQDTLPLCPL WISRQFREAA
PLCQDGTCSA EQLALMLAQR EWREGYLAER MQDEILQEQI LIETEGERIG QINALSVIEF
PGHPRAFGEP SRISCVVHIG DGEFTDIERK AELGGNIHAK GMMIMQAFLM SELQLEQQIP
FSASLTFEQS YSEVDGDSAS MAELCALISA LSNVPVNQNI AITGSVDQFG RAQPVGGLNE
KIEGFFTICQ QRELTGKQGV IIPAANVRHL SLQPALLQAV EEEKFSIWAV DDVTDALPLL
LNLVWDGEGQ TTLMQTIQER IAQATQQEGR HRFPWPLRWL NWFIPN
//
