ID   LTRB_LACLM              Reviewed;         563 AA.
AC   Q48665; A2RKZ4;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Group II intron-interrupted relaxase LtrB;
DE   AltName: Full=Conjugative nickase;
DE   AltName: Full=Mobilization protein MobA;
GN   Name=ltrBE1; Synonyms=mobAE1; OrderedLocusNames=llmg_1372;
GN   and
GN   Name=ltrBE2; Synonyms=mobAE2; OrderedLocusNames=llmg_1370;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8843433; DOI=10.1046/j.1365-2958.1996.00610.x;
RA   Shearman C., Godon J.-J., Gasson M.;
RT   "Splicing of a group II intron in a functional transfer gene of Lactococcus
RT   lactis.";
RL   Mol. Microbiol. 21:45-53(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
CC   -!- FUNCTION: Mediates initiation of conjugal transfer possibly by
CC       introducing a single-stranded nick at the potential origin of transfer.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC   -!- MISCELLANEOUS: The gene coding for this protein is interrupted by a
CC       group II intron, IntL. Splicing of the intervening intron is necessary
CC       for proper protein activity and, therefore, conjugative transfer, as
CC       the splicing event brings together the two conserved histidine residues
CC       proposed to function as ligands for the metal ion cofactor.
CC   -!- SIMILARITY: Belongs to the mobilization (MOB) protein type 1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA61995.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=CAL97960.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; X89922; CAA61995.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AM406671; CAL97960.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S77647; S77647.
DR   RefSeq; WP_011835236.1; NC_025249.1.
DR   RefSeq; YP_009091785.1; NC_025249.1.
DR   AlphaFoldDB; Q48665; -.
DR   SMR; Q48665; -.
DR   STRING; 416870.124492997; -.
DR   EnsemblBacteria; CAL97960; CAL97960; CAL97960.
DR   eggNOG; COG3843; Bacteria.
DR   HOGENOM; CLU_031118_4_2_9; -.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR005094; Endonuclease_MobA/VirD2.
DR   Pfam; PF03432; Relaxase; 1.
PE   3: Inferred from homology;
KW   Conjugation; Magnesium; Manganese; Metal-binding; Mobility protein.
FT   CHAIN           1..563
FT                   /note="Group II intron-interrupted relaxase LtrB"
FT                   /id="PRO_0000084515"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000255"
FT   BINDING         159
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   563 AA;  64870 MW;  BB1A204177662CE7 CRC64;
     MVYTKHIIVH KLKHLRQAKD YVENAEKTLV NESNEDHLTN LFPYISNPDK TMSKQLVSGH
     GITNVYDAAN EFIATKKLKA LSKGTDFNFD PQTGKVRFNV ESLEKNNAVL GHHLIQSFSP
     DDNLTPEQIH EIGRQTILEF TGGEYEFVIA THVDREHIHN HIIFNSTNLY TGKQFDWKVI
     PKEKTKSGKA YDVTKNNFEK VSDKIASRYG AKIIEKSPGN SHLKYTKWQT QSIYKSQIKQ
     RLDYLLEMSS DIEDFKRKAT ALNLSFDFSG KWTTYRLLDE PQMKNTRGRN LDKNRPEKYN
     LESIIERLET NELSLTVDEV VERYEEKVDV VKQDFDYQVT VEKGQIDHMT SKGFYLNVDF
     GIADRGQIFI GGYKVDQLEN RDCVLYLKKN ETFRLLSEKE ASFTKYLTGH DLAKQLGLYN
     GTVPLKKEPV ISTINQLVDA INFLAEHGVT EGTQFNNMES QLMSALGEAE EKLYVIDNKI
     MELTKIAKLL IEKESDHSQA VINELENLGV GPSIKYQDIH QELQSEKMSR KILKNKFEQT
     VDEINTFNEI RVTTLEENKG KIL