ID A0A0Q9LAT9_9BACL Unreviewed; 1012 AA.
AC A0A0Q9LAT9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Archaeal Lon protease {ECO:0000256|ARBA:ARBA00022016};
GN ORFNames=ASG81_05820 {ECO:0000313|EMBL:KRE49051.1};
OS Paenibacillus sp. Soil522.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE49051.1, ECO:0000313|Proteomes:UP000051180};
RN [1] {ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE49051.1, ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE49051.1,
RC ECO:0000313|Proteomes:UP000051180};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
CC subfamily. {ECO:0000256|ARBA:ARBA00009579}.
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:KRE49051.1}.
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DR EMBL; LMRV01000027; KRE49051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9LAT9; -.
DR STRING; 1736388.ASG81_05820; -.
DR OrthoDB; 9782629at2; -.
DR Proteomes; UP000051180; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd02145; BluB; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.109.10; NADH Oxidase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012825; BluB.
DR InterPro; IPR004663; Lon_arc.
DR InterPro; IPR046843; LonB_AAA-LID.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR002078; Sigma_54_int.
DR NCBIfam; TIGR02476; BluB; 1.
DR NCBIfam; TIGR00764; lon_rel; 1.
DR PANTHER; PTHR23026:SF90; IODOTYROSINE DEIODINASE 1; 1.
DR PANTHER; PTHR23026; NADPH NITROREDUCTASE; 1.
DR Pfam; PF20436; LonB_AAA-LID; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR Pfam; PF00881; Nitroreductase; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF55469; FMN-dependent nitroreductase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 294..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 219..482
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 1012 AA; 112542 MW; 61AEE2537668D077 CRC64;
MNRFVIRLFA SALDHYARKG KVVAMERTIA LIIRYFEKQP EQWIEALYLF SKDTRWILRY
LAGREIGRLI VYDQVEAAGI AMRLAGDSSL YVREGIAKGI VQSAIAGFDQ VWQFWQKAFD
DHSDEVRQTA AMTLISLLNM PEIKMKLLPE AEKIRHDGSV KVKAIFDNYV APILDEQSSA
AEQRSDYATT AEVPVPKRII DQVVGQDEAV FIIRLAASQK RSVLLIGEPG TGKSMLGRAM
AELLHGTHLT DVVVEVGVKE RSIPSIRLMP AGEGERFIKE YEHSHRTNAA SLRWILGFAA
FVCLFVTVFY SFTRDNPVYM MSGLLILLII FWFGKTLKIT PNNKTPKYLI NNSGKENPPF
IDATGLHAGA LLGDVRHDPY QSGGMETSPH HLVEPGAIHL AHQGVLYIDE VSTLSLESQQ
ALLTAFQEKK MAITGRTPGS SGRMIRTEPV PSDFILVLAG NMQDVEKIHP ALRSRIRGYG
YEVYLNDTMP DTAENRFKLF QFVAQEVHRD GKIPHFTSAA VNEVIHQASR KADRAGYLSS
RFRELGGLIR AAGDAAVQSG SALVYKDHIL KALNISIPLE EQIALREYGS LKLLRVDSCC
GRVKALASNQ DAFGTMVVQC WTDFQPSRAV EINTAAGDGP GNPDVSPIEA ALNRFRLPGK
YFIEIEGAES NHSFKHFSLA IALSALSAAH ESILPEYLAV CGSINVLGLV KESRYFDRTI
AAAQHSGIRT LIAPIGNRRA ELPGEIQFIW VHSLDEAWHA VQSQSAALAL PIKEAAAQPV
QQSVSRGHSL TDIPRTDFAF TEQDKAAVYR AIEQRRDIRS FKPDPVSDEL LKRLLTAAHH
APSVGYMQPW NFIVIKSEVT KQKLKGVADK ERRALMVHYE GEKANKFSKL KIEGLTEAPI
TLCVTLDPTR GGPHVFGRNS IPETDLASVS CAIQNLWLAA RAEGLAAGWV SFYKKQDVRG
VLDIPPHVDP VALISIGYTD EFPDQPILQK ENWRKRIPLE ELIYSEFWGK EG
//
