ID D5E538_MYCCM Unreviewed; 873 AA.
AC D5E538;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN Name=lon {ECO:0000313|EMBL:ADE19648.1};
GN OrderedLocusNames=MCRO_0227 {ECO:0000313|EMBL:ADE19648.1};
OS Mycoplasma crocodyli (strain ATCC 51981 / MP145).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=512564 {ECO:0000313|EMBL:ADE19648.1, ECO:0000313|Proteomes:UP000001845};
RN [1] {ECO:0000313|Proteomes:UP000001845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RA Glass J.I., Durkin A.S., Hostetler J., Jackson J., Johnson J., May M.A.,
RA Paralanov V., Radune D., Szczypinski B., Brown D.R.;
RT "The complete genome of Mycoplasma crocodyli MP145.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MP145;
RA Ma Z., Wang X., Liu H.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADE19648.1, ECO:0000313|Proteomes:UP000001845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RX PubMed=21460083; DOI=10.1128/JB.00309-11;
RA Brown D.R., Farmerie W.G., May M., Benders G.A., Durkin A.S., Hlavinka K.,
RA Hostetler J., Jackson J., Johnson J., Miller R.H., Paralanov V., Radune D.,
RA Szczypinski B., Glass J.I.;
RT "Genome sequences of Mycoplasma alligatoris A21JP2T and Mycoplasma
RT crocodyli MP145T.";
RL J. Bacteriol. 193:2892-2893(2011).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; CP001991; ADE19648.1; -; Genomic_DNA.
DR RefSeq; WP_013054424.1; NC_014014.1.
DR AlphaFoldDB; D5E538; -.
DR STRING; 512564.MCRO_0227; -.
DR MEROPS; S16.001; -.
DR KEGG; mcd:MCRO_0227; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_5_2_14; -.
DR OMA; KKMNPVM; -.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000001845; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
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 NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF56; LON PROTEASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
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:ADE19648.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000001845};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 673..854
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 760
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 803
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 873 AA; 99290 MW; 281DF7BDE488CCC7 CRC64;
MLLPFIITKL EHISLPNVVY TAEIEEGHQH DEFLSSVESL TFDRIVIAYT DASKPGKNAS
LNGYGLYVKP LKLFRKNKKL FITYKGIEVL NLLHTPYSFK ESDLSEADAK TFLKNPEFYI
KNMVCEKISK SNKSSDISDP FEMGENVTSF LTMLKQSYKA LEDMKESILK INPENGKQYK
MVDILNAQKF DKEPGFRIED YPEIFLNTIL SYTKKIDGFW DLNEYLILQD PKDQFTYATN
IARYASKVIE VETEIQSNME DSMLQQQKEF MLREKIKAIK SQLETMDSTE SEEDEYKKLI
KNKKTAKIYP ESVQKIIKDE NERYSQMMAS SPDANITRTY IETLKKLPWR KTEINYLDIK
KAREVLDKHH YGLDEVKERI IEHLAVILNN RKHNNNSKNL IPLDSEHEID LELFKQIKVK
DGDNTYNNVP ILALVGPPGT GKTSLSKAIA EALQKSFVKI SLGGVHDESE IRGHRRTYVG
AMPGKIVKSF LKCEVSNPLI LLDEIDKMAS DTKGDPASAM LEVLDPEQNS KFQDHYLEHE
YDLSKVMFIA TANEHDGIPA PLLDRVEIIE LSPYTITEKI KIAKQHLINK VLEQTSLTPE
LFKIDDDTLK YIIKHYTLEA GVRGLKRLLD KIARKIVVKV IDDPKLKKFE IKKEMLIDLI
GIVKFKEEER EVEEVKGTVT GLAYSIAGGS TLQIEVTAYP GKGEIKLTGQ LKDVMQESAQ
IALTYVRANA SKFGINDFDF EGNTIHIHVP EGAIPKDGPS AGVTFTTAII SALSGKTVKN
IYGMTGEITL RGKVLEIGGL KEKSFAATQK GLTHVFIPYN NIKNLKDIPD EIKDLLIYIP
VKKYSEIYDV IFNGKKPEIT IDKSNNKKLS VFY
//