ID A0A1F1UVG2_9CORY Unreviewed; 362 AA.
AC A0A1F1UVG2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=HMPREF3170_05235 {ECO:0000313|EMBL:OFT30087.1};
OS Corynebacterium sp. HMSC08D02.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581138 {ECO:0000313|EMBL:OFT30087.1, ECO:0000313|Proteomes:UP000177600};
RN [1] {ECO:0000313|EMBL:OFT30087.1, ECO:0000313|Proteomes:UP000177600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08D02 {ECO:0000313|EMBL:OFT30087.1,
RC ECO:0000313|Proteomes:UP000177600};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFT30087.1}.
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DR EMBL; LWNU01000021; OFT30087.1; -; Genomic_DNA.
DR RefSeq; WP_070478292.1; NZ_KV789242.1.
DR AlphaFoldDB; A0A1F1UVG2; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000177600; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
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:SF48; ENDOPEPTIDASE LA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Reference proteome {ECO:0000313|Proteomes:UP000177600};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 254..352
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 362 AA; 37852 MW; 70B281F6564EF488 CRC64;
MNAEQEQAQA QPRSRRLATI VWGAIPLAVL AAALSLDHIP GTDISLAVPY AAQGPGPTFN
TLGDVEGVPV VEIEGADSDE TEGNLNMTTV SVRTNMTLVQ ALTRWITTDD TIVPLEQIMP
PNTNREEMKQ RNQEAFVASE SAATIAAMNY LGRPTTVVVH EVMEGSAANG ALQAADIITK
VGGKDVSQPR QVQQIVREHA PGDRLSVDVL RDGAPHTEEI TLGANPEDKK VPMLGILMTS
APADGVQVTY NLNDVGGPSA GMMFSLAVID KLSPGLLNGG KFVAGTGTID ESGEVGPIGG
ISHKIAGARD AGAELFLAPE GNCAEVMRTD SGEMQVAAVK TLDDAVKAMD AFAHGQPVRS
CS
//
