ID G9XSX4_DESHA Unreviewed; 652 AA.
AC G9XSX4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=HMPREF0322_04078 {ECO:0000313|EMBL:EHL05339.1};
OS Desulfitobacterium hafniense DP7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=537010 {ECO:0000313|EMBL:EHL05339.1, ECO:0000313|Proteomes:UP000004416};
RN [1] {ECO:0000313|EMBL:EHL05339.1, ECO:0000313|Proteomes:UP000004416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP7 {ECO:0000313|EMBL:EHL05339.1,
RC ECO:0000313|Proteomes:UP000004416};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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:EHL05339.1}.
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DR EMBL; AFZX01000105; EHL05339.1; -; Genomic_DNA.
DR RefSeq; WP_005815189.1; NZ_JH414485.1.
DR AlphaFoldDB; G9XSX4; -.
DR MEROPS; S16.A11; -.
DR PATRIC; fig|537010.4.peg.3811; -.
DR HOGENOM; CLU_020014_0_0_9; -.
DR Proteomes; UP000004416; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
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 InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR014252; Spore_LonC.
DR NCBIfam; TIGR02903; spore_lon_C; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF64; 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.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 208..391
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 480..652
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 563
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 606
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 652 AA; 71906 MW; 10DB644280D3FE6A CRC64;
MKGLLNHWFK KNETEPIQEA EETNQPSSQV EELKEDVRNS HEQWHHEVDA LYSLLVNYYG
SDKLVLKATR LEAIHLIQSD TIGERTAGLL KIILDDPTDR PLPSEEEIPQ LLMEIEDHLA
ELIARRAVED RLDKAVADKM QERHEDYVKE IKSQLLKENS GPDNAQTLKK LAHIEKMNLV
KLASSVAEVL RPQAVEEIIG QEVPMQFLLA KLATPYPQHI IIYGPPGVGK TSAARVALEA
VKKNVNSPFA ESAPFVEVDG TTLRWDPRDV TNPLLGSVHD PIYQGAKRDL AETGIPEPKL
GLVSDAHGGI LFIDEIGEMD PVLLNKLLKV LEDKRVAFES AYYDPNDPQV PLYIKKLFEE
GAPADFVLIG ATTRDPRELN PALRSRCGEI YFNPLEPRDI QHIVSQAAQK LGANLEAKVP
EVISEYVFEG RKANTILTDA YGLSRYRHPE QEVLVKAEEV YEVLRSARLT PYISHKAADR
GETGKILGLG VHGFVGSVLE LEAIVFPGRE GKGTIRFNET AGSMARDAVF NATAVIRSLT
GEDLKDYDVH VNVVGGGNID GPSAGCATTL AIYSALKNIP LRQDIAVTGE ISIQGRVRPV
GGIAEKIFGA KQAGVKTVLI PKENQADVPS GLQGIQVIPI ETFREALEHA LF
//
