ID   LACTB_BOVIN             Reviewed;         556 AA.
AC   P83095;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Serine beta-lactamase-like protein LACTB, mitochondrial {ECO:0000305};
DE            EC=3.4.-.- {ECO:0000250|UniProtKB:P83111};
DE   Flags: Precursor;
GN   Name=LACTB {ECO:0000250|UniProtKB:P83111};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 402-416; 432-463 AND 467-476, AND SUBCELLULAR LOCATION.
RC   TISSUE=Liver {ECO:0000269|PubMed:11551941};
RX   PubMed=11551941; DOI=10.1074/jbc.m106510200;
RA   Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M.,
RA   Moseley A., Spremulli L.L.;
RT   "The large subunit of the mammalian mitochondrial ribosome. Analysis of the
RT   complement of ribosomal proteins present.";
RL   J. Biol. Chem. 276:43958-43969(2001).
CC   -!- FUNCTION: Mitochondrial serine protease that acts as a regulator of
CC       mitochondrial lipid metabolism. Acts by decreasing protein levels of
CC       PISD, a mitochondrial enzyme that converts phosphatidylserine (PtdSer)
CC       to phosphatidylethanolamine (PtdEtn), thereby affecting mitochondrial
CC       lipid metabolism. It is unclear whether it acts directly by mediating
CC       proteolysis of PISD or by mediating proteolysis of another lipid
CC       metabolism protein. {ECO:0000250|UniProtKB:P83111}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11551941}.
CC   -!- SIMILARITY: Belongs to the peptidase S12 family. {ECO:0000305}.
CC   -!- CAUTION: Was originally identified as 39S ribosomal protein L56 (MRP-
CC       L56). {ECO:0000305|PubMed:11551941}.
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DR   AlphaFoldDB; P83095; -.
DR   SMR; P83095; -.
DR   STRING; 9913.ENSBTAP00000023098; -.
DR   PaxDb; P83095; -.
DR   PRIDE; P83095; -.
DR   eggNOG; ENOG502QQBX; Eukaryota.
DR   HOGENOM; CLU_020027_6_0_1; -.
DR   InParanoid; P83095; -.
DR   TreeFam; TF315050; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.710.10; -; 2.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   Pfam; PF00144; Beta-lactamase; 2.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Hydrolase; Lipid metabolism;
KW   Mitochondrion; Protease; Reference proteome; Transit peptide.
FT   TRANSIT         1..117
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           118..556
FT                   /note="Serine beta-lactamase-like protein LACTB,
FT                   mitochondrial"
FT                   /id="PRO_0000262964"
FT   REGION          249..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        166
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P15555"
FT   MOD_RES         290
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EP89"
FT   MOD_RES         291
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EP89"
FT   MOD_RES         304
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EP89"
FT   MOD_RES         349
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P83111"
SQ   SEQUENCE   556 AA;  61683 MW;  029D06A48ACA8852 CRC64;
     MYRLLSAVMA RAATTGGCAW GCGRRAAHQR AGLPPLGPGW VGGLGLGLGL ALGVKLAGGL
     RGASPAPPAA APDPEALPQA EPLQAQEQPL APWSPQTPAP PHTRHFARAI DSSRDLLHRI
     KDEVGAPGIV VGVSVDGKEV WSEGLGYADV ENRVPCKPET VMRIASISKS LTMVAIAKLW
     EAGKLDLDIP VQHYVPEFPE KEYEGEKVSV TTRLLISHLS GIRHYEKDMK KVKEEKAYKA
     LKMMKEMMES DQEKELKEKG GKSNEKNDFA KAKVEQDNET KGRNSKPCKK KNDFEQGELY
     LKEKFENSIE SLRLFKNDPL FFKPGSQFLY STFGYTLLAA IVERASGYKY LDYMQKIFHD
     LDMLTTVQEE NEPVIYNRAR FYVYNKKKRL VNTPYVDNSY KWAGGGFLST VGDLLKFGNA
     MLYGYQVGLF KNANENLLPG YLKPETMLMI WTPVPNTEMS WDKEGKYAMA WGVVEKKQTY
     GSCRKQRHYA SHTGGAVGAS SVLLVLPEEL DAEALNNKVP PRGIVVSIIC NMQSVGLNST
     ALKIALEFDK DRSDIP