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Database: UniProt
Entry: A0A448V0G1_9FIRM
LinkDB: A0A448V0G1_9FIRM
Original site: A0A448V0G1_9FIRM 
ID   A0A448V0G1_9FIRM        Unreviewed;       407 AA.
AC   A0A448V0G1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel insertion protein {ECO:0000256|HAMAP-Rule:MF_01074};
DE            Short=P2TMN nickel insertion protein {ECO:0000256|HAMAP-Rule:MF_01074};
DE            EC=4.99.1.12 {ECO:0000256|HAMAP-Rule:MF_01074};
DE   AltName: Full=Nickel-pincer cofactor biosynthesis protein LarC {ECO:0000256|HAMAP-Rule:MF_01074};
GN   Name=larC {ECO:0000256|HAMAP-Rule:MF_01074};
GN   ORFNames=NCTC13079_00331 {ECO:0000313|EMBL:VEJ34801.1};
OS   Peptoniphilus ivorii.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=54006 {ECO:0000313|EMBL:VEJ34801.1, ECO:0000313|Proteomes:UP000269544};
RN   [1] {ECO:0000313|EMBL:VEJ34801.1, ECO:0000313|Proteomes:UP000269544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13079 {ECO:0000313|EMBL:VEJ34801.1,
RC   ECO:0000313|Proteomes:UP000269544};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of a nickel-pincer cofactor
CC       ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel
CC       delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide
CC       (P2TMN), to form the mature cofactor. Is thus probably required for the
CC       activation of nickel-pincer cofactor-dependent enzymes.
CC       {ECO:0000256|HAMAP-Rule:MF_01074}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide =
CC         Ni(2+) + pyridinium-3,5-bisthiocarboxylate mononucleotide;
CC         Xref=Rhea:RHEA:54784, ChEBI:CHEBI:49786, ChEBI:CHEBI:137372,
CC         ChEBI:CHEBI:137373; EC=4.99.1.12; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01074};
CC   -!- SIMILARITY: Belongs to the LarC family. {ECO:0000256|HAMAP-
CC       Rule:MF_01074}.
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DR   EMBL; LR134523; VEJ34801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A448V0G1; -.
DR   KEGG; piv:NCTC13079_00331; -.
DR   OrthoDB; 9765625at2; -.
DR   Proteomes; UP000269544; Chromosome 1.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051604; P:protein maturation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.1380; Transcriptional regulatory protein pf0864 domain like; 1.
DR   HAMAP; MF_01074; LarC; 1.
DR   InterPro; IPR002822; Ni_insertion.
DR   NCBIfam; TIGR00299; nickel pincer cofactor biosynthesis protein LarC; 1.
DR   PANTHER; PTHR36566; NICKEL INSERTION PROTEIN-RELATED; 1.
DR   PANTHER; PTHR36566:SF1; NICKEL INSERTION PROTEIN-RELATED; 1.
DR   Pfam; PF01969; Ni_insertion; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01074};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269544}.
FT   REGION          71..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  44765 MW;  62B14393D19C7E70 CRC64;
     MRALYIDPFS GISGNMYIGA LLDMGAEIGP FLEGIAPLGV TVEDILLKKV DRKGIRATYF
     NLKGEEEKLR AHEHEHAHHH EHEHGHTHNH THGGHRTLAD VMDCIDKSAF DDEVKILAKA
     IYMPLARAEA AIHGKCLADV HFHEVGETDA IVDVLGAAYF TFAWDVEEIY VGKINAGFGT
     VHCAHGNYPL PAPATAKILA DLNAPLGGMP VETELTTPTG AAILKGIGAQ YRPMPEGRIL
     KSAYGAGTKD GAWANVLRVL LLETEEAEAP IWYSCNIDDM TGEELGFCME KLFEAGAKDV
     TFTPIYMKKN RPGQRIDVLG ARADAEALKE ILFTHTTTLG IKEIPLEKIE LARTVESGTI
     GTWAVRTKTA RYGDRKKASP EYEDLRALAT EEDISLRAAY GLWERRR
//
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