ID A7B8V8_9ACTO Unreviewed; 415 AA.
AC A7B8V8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Lon proteolytic domain-containing protein {ECO:0000259|Pfam:PF05362};
GN ORFNames=ACTODO_00058 {ECO:0000313|EMBL:EDN79632.1};
OS Schaalia odontolytica ATCC 17982.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=411466 {ECO:0000313|EMBL:EDN79632.1, ECO:0000313|Proteomes:UP000003553};
RN [1] {ECO:0000313|EMBL:EDN79632.1, ECO:0000313|Proteomes:UP000003553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17982 {ECO:0000313|EMBL:EDN79632.1,
RC ECO:0000313|Proteomes:UP000003553};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDN79632.1, ECO:0000313|Proteomes:UP000003553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17982 {ECO:0000313|EMBL:EDN79632.1,
RC ECO:0000313|Proteomes:UP000003553};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Actinomyces odontolyticus (ATCC 17982).";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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:EDN79632.1}.
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DR EMBL; AAYI02000004; EDN79632.1; -; Genomic_DNA.
DR AlphaFoldDB; A7B8V8; -.
DR MEROPS; S16.012; -.
DR eggNOG; COG3480; Bacteria.
DR HOGENOM; CLU_042037_1_0_11; -.
DR Proteomes; UP000003553; 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:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
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 SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 307..398
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|Pfam:PF05362"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 43622 MW; 0D5D51C7491F9836 CRC64;
MARGARAQGQ RVGHNDTVND AQMTSENIEL VPLQEDDSTR RIPIVSWRIV TAVLAALAMV
VILFWIPVPF VVNSPGPTFN VLGSDNGVPM LQIEGTDPTT GEAIEQDEPQ STSYKAPAKP
GQGQLRMVTV SESGNPKSRL NFAQLIAAYF DPHSKIVDYE SVYPKGLTQE RSSAAQLAMM
RNSQTTSQVA ALEYLGWEVP ATVTIEGAVE GTNAEGIVQQ GDILRAITTP DGVRHEITSA
ATPFALMRSV PAGSTMTLTI EREGATQDVS FASVAASANE SGSKLGVYLS VDPALPVDIT
VNIDGVGGPS AGMMFSLSII DRLTPGDMTG GKVIAGTGTM SYDGQVGGIG GIQQKLWGAH
RDGAQWFLAP SENCNEVVGH VPDGLRVVSV STLDEAVNAV RSIADGTGDA LPTCQ
//
