ACL_RS02690

Uniprot: A9NFM4
Description: endopeptidase La
EC number: 3.4.21.53
Annotation score: 3 out of 5
Miscellaneous [CC]:
Protein existence: Evidence at transcript level
Catalytic activity: CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP. {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00004348}.
Cofactor:
Enzyme regulation:
Function [CC]: FUNCTION: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00338846}.
Pathway:
Active site: ACT_SITE 676 676 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRSR:PIRSR001174-1}.; ACT_SITE 719 719 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRSR:PIRSR001174-1}.
Binding site:
Calcium binding:
DNA binding:
Metal binding:
Nucleotide binding: NP_BIND 353 360 ATP. {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRSR:PIRSR001174-2}.
Site:
Gene names (primary): lon
Gene names (synonym):
Mass: 86,693
Subunit structure [CC]: SUBUNIT: Homohexamer. Organized in a ring with a central cavity. {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00536021}.
Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; ATP-dependent peptidase activity [GO:0004176]; sequence-specific DNA binding [GO:0043565]; serine-type endopeptidase activity [GO:0004252]; cellular response to stress [GO:0033554]; misfolded or incompletely synthesized protein catabolic process [GO:0006515]
Gene ontology IDs: GO:0004176; GO:0004252; GO:0005524; GO:0005737; GO:0006515; GO:0033554; GO:0043565
Chain:
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|RuleBase:RU000591, ECO:0000256|SAAS:SAAS00536024}.; SIMILARITY: Contains 1 Lon N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01973}.; SIMILARITY: Contains 1 Lon proteolytic domain. {ECO:0000256|HAMAP-Rule:MF_01973}.
Protein families: Peptidase S16 family
Coiled coil:
Domain [FT]: DOMAIN 6 199 LON. {ECO:0000259|SMART:SM00464}.; DOMAIN 345 490 AAA. {ECO:0000259|SMART:SM00382}.
Motif:
Region:
EMBL: CP000896
ProteinModelPortal: A9NFM4
MEROPS: S16.001
EnsemblBacteria KO: ABX81154
UniPathway: K01338
CDD:
Gene3D:
HAMAP: 3.30.230.10;3.40.50.300
InterPro: MF_01973
PANTHER: IPR003593;IPR003959;IPR027543;IPR004815;IPR027065;IPR003111;IPR027417;IPR008269;IPR008268;IPR015947;IPR020568;IPR014721
PIRSF: PTHR10046
PRINTS: PIRSF001174
PROSITE:
Pfam: PS01046
ProDom: PF00004;PF05362;PF02190
SMART:
SUPFAM: SM00382;SM00464
TIGRFAMs: SSF52540;SSF54211;SSF88697

570426-572739(+)

>nucleotide sequence
ATGGAATTACAGACAAGTTTACCCGCGATTGTTGTACGTGGTATCGTACCGATTCCTAAT
AATGATTTTAGAATTGAAGTTGGCCGTAAAGTATCCCTTAAAGCGATTGAAGAGTCTGAA
AAGAGTTTTTCATCTTACGTACTTATATTGGTTCAAAAAAATCCATTAATAGAAAACCCA
ACAGTTGCTGATATTGAAACTCATGGTGTCTTAGCTAAGATTGCTATGAAGATTAAATTA
CCTAATAACAACTATAAAATTAAGTTTAATTTAATGTCTAGAATTAAAGTCAATGAGTAC
TTTTTAACAGATCCTTACTTTGTAGCAGACTATGAAGAATTAGAATCAAAAGTAGGGGAA
ATTGAAGAAGAAACTACATTACTTAAATTAATTACTGATGAAGCTGTTGTAAATGCAAAT
CAGTTGTTTAATAATGCCCAAGTGATTACATCACAAATTCAATCTGGTTTATCATCAGAT
AAAATGGCGGACATTTTAGCATATAATTTAAGAACTCAAGATACTGAAAAATATAAGTAT
CTAGCTGAATTAAATGTAAATTCAAGACTAAAATTAATTTTAGAAGATATTAACCGTCTA
AAGATGATTGCTGATTTAGAACAGCGTATTAATGAAGATGTTAAAAAGGCAATTGATGAA
AATCAAAAAGAATATTATTTAAGAGAAAAAATGCGTGCAATTCAAAATGAATTAGGTGAT
AAAGCTAAAAAAGAAGATGAAATTGATAAATTAAGAGAAGATATTAAGAAGGCTAAAATG
CCGCTTCATATCGAAGAAAAGGCCCTACAAGAGCTATCTCGTTATCAATCAACACCTTCA
GCAATGGCTGAATCTCAAATTATTAAAACTTACCTAGATTTTCTAGTTGCATTACCTTGG
AATGAATCATCAACAGATTTAAATGATTTACAAAAGGTACAAGATAACTTAGATAAGAAT
CATTATGGTCTGGAAAATGTTAAAGAACGTATTATTGAATATCTAGCAGTTAAGATGATG
ACTGGTAGAAATCCACAGACTATTTTATGTTTAGCAGGTCCTCCAGGGGTTGGTAAAACA
TCACTTGCAACATCTATTGCAGAAGCTTTAGGTCGTAAGTTTGTTAAACAATCACTAGGT
GGCGTTAAAGATGAATCAGAAATACGTGGTCATAGAAGAACTTACGTAGGCGCTATGCCT
GGTCGTATCCTTAAGGGTATGAAGGATGCTGGTACAGTAAATCCTGTCTTCTTATTAGAT
GAAATTGATAAAATGGCATCTGATTATAGAGGGGACCCTGCATCTGCAATGCTTGAAGTA
TTAGACCCAGAGCAAAATGCTAAATTTAGTGATCACTACTTGGAAGAAAATTATGACTTA
TCTCAAGTATTATTCATTACAACAGCAAACTATCTTGAAAATGTGCCTGCACCTTTAAGA
GATCGTATGGAAATTGTAGAACTATCTAGCTATACTGAGTATGAAAAAATTCAGATTGCT
CAAAAACACTTAGTTAACAAACAATTATCAGCACACGGTTTAGATAGTGATAAATTTACA
ATTGATGAAGAAACACTTTACTTTATTGTAAGACATTACACTAGAGAAGCTGGTGTTCGT
GAGTTAAACCGTTATATTGGTTCTTTAGTACGTAAAGCAATTAAAGAAATTCTTATGAAA
AAAGCAGATAAAATTCATATCACTAAAGAAAATGTAGAAACATATATAGGTAAACCTAAG
TTTGTACATAATTTAGTGGATGAAAAACAACAAATTGGTGTTGTGACTGGTCTAGCATAT
ACTGCATTTGGTGGAGACACACTTCCGGTTGAAGTTACTTACTATAAAGGTAAGGGACAA
CTTGTTTTAACAGGTAAACTAGGGGATGTCATGAAAGAATCAGCAATTACTGCACTTTCA
TATGTAAAATCACATGCACTAGAATTTAATTTAGACCCAACGATATTTGAAAACAACGAC
TTCCACGTCCACGTACCAGAAGGAGCAATTCCTAAAGATGGTCCTTCAGCGGGTATTACC
ATGGCAACTGCGATTATGTCAGCTGCAAGTAAACTCTATGTTAGAAAAGACCTTGGTATG
ACCGGTGAAATTACATTACGCGGTTATGTACTACCAATTGGTGGATTAAAAGAAAAAGCA
ATTGCTGCTTTAAGAAGTGGTTTAACTACTATTTTAATTCCAAAACAAAACGTTAAAGAT
GTTGATGATATTCCAAAAGAAGTTAGAGACAAATTAACAATTATTCCTGTTGAAAATGTA
TCTGATGTTTTTGCACAAGCATTGATTAGATAA

>protein sequence
MELQTSLPAIVVRGIVPIPNNDFRIEVGRKVSLKAIEESEKSFSSYVLILVQKNPLIENP
TVADIETHGVLAKIAMKIKLPNNNYKIKFNLMSRIKVNEYFLTDPYFVADYEELESKVGE
IEEETTLLKLITDEAVVNANQLFNNAQVITSQIQSGLSSDKMADILAYNLRTQDTEKYKY
LAELNVNSRLKLILEDINRLKMIADLEQRINEDVKKAIDENQKEYYLREKMRAIQNELGD
KAKKEDEIDKLREDIKKAKMPLHIEEKALQELSRYQSTPSAMAESQIIKTYLDFLVALPW
NESSTDLNDLQKVQDNLDKNHYGLENVKERIIEYLAVKMMTGRNPQTILCLAGPPGVGKT
SLATSIAEALGRKFVKQSLGGVKDESEIRGHRRTYVGAMPGRILKGMKDAGTVNPVFLLD
EIDKMASDYRGDPASAMLEVLDPEQNAKFSDHYLEENYDLSQVLFITTANYLENVPAPLR
DRMEIVELSSYTEYEKIQIAQKHLVNKQLSAHGLDSDKFTIDEETLYFIVRHYTREAGVR
ELNRYIGSLVRKAIKEILMKKADKIHITKENVETYIGKPKFVHNLVDEKQQIGVVTGLAY
TAFGGDTLPVEVTYYKGKGQLVLTGKLGDVMKESAITALSYVKSHALEFNLDPTIFENND
FHVHVPEGAIPKDGPSAGITMATAIMSAASKLYVRKDLGMTGEITLRGYVLPIGGLKEKA
IAALRSGLTTILIPKQNVKDVDDIPKEVRDKLTIIPVENVSDVFAQALIR