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Database: UniProt
Entry: D5E538_MYCCM
LinkDB: D5E538_MYCCM
Original site: D5E538_MYCCM 
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
//
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