ID K6XBT4_9ALTE Unreviewed; 795 AA.
AC K6XBT4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=GARC_1113 {ECO:0000313|EMBL:GAC18094.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC18094.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC18094.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC18094.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC18094.1}.
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DR EMBL; BAEO01000013; GAC18094.1; -; Genomic_DNA.
DR RefSeq; WP_007617554.1; NZ_BAEO01000013.1.
DR AlphaFoldDB; K6XBT4; -.
DR STRING; 493475.GARC_1113; -.
DR eggNOG; COG1067; Bacteria.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000006327; Unassembled WGS sequence.
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 Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR046844; Lon-like_helical.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR046843; LonB_AAA-LID.
DR InterPro; IPR027417; P-loop_NTPase.
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:SF49; LON PROTEASE HOMOLOG-RELATED; 1.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF20436; LonB_AAA-LID; 1.
DR Pfam; PF20437; LonC_helical; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000006327};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 563..758
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 202..229
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 653
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 696
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 795 AA; 89305 MW; C806BC7014C3AFC9 CRC64;
MQSKYALHLQ QLTAKPSRRL INQALKDQDA LNSTFIGQDR ARDALSFGLG IDARGYNLYV
MGEQATGRFT LVHEFIDKYV SKTVTPDDWC YINNFEDERE PFSLRLKAGE SKNLSKDLEN
LVDELLDTFP AAFDNPGYQR KKAAITREFD QGYDKAIDEV EKLAQQQSVA LNEDGGTITF
SPIVDGNLVS DEDFAKVSDQ ERQHYYQLID DLEKKLSEAL IELPKWKRAT AEKLRSLKKE
TAEQGIKPLL KDLEHKYSSD LAILKFLRQL KPHLVETVVE VLADDKKDEK HDEYDKRSIL
EEQYLPNIIV SHELNSGSPV VYEPNPTHQN LFGRVEYTNI QGSVFTNYRM IRPGAMHRAN
GGYLLLDVDK LIEQPFAWET LKLVLKFGSL KMDLPQHEVG MVNSITLNPQ QIPIDVKVIL
LGSRDLYYTL QDYDDEFYEL FRVLVDFDHE IPLDKKTLFD FVGRVRIQVK ELGLHSISAK
AMYRLVEYSL RLAEHQQRLS ARFSDVIELL HEAEYFCRQK HSQELDVTHL ESALAAKTHR
TGRVSEAVLD DIKQGQILIA TQGIDVGKVN GLTVLEIGDS MFGTPARITS TVYAGANGVV
DIEREVELGQ PSHSKGVMLL TGYLGHKYAQ LFPLTLSANI AIEQSYGHID GDSASLAELV
ALISALTKMP VRQDLAITGS INQYGQVQSV GGVNEKIEGF FKLCQHRGLT GTQGVIIPKS
NQVNLMLDKE VLAAVKAQKF HICVVETVDD ALTLLMDKEA GVHNTKGRYP KGSVNYMAVS
SLLNIANIVA GADDE
//
