ID A0A1Y5KIS6_9BACL Unreviewed; 511 AA.
AC A0A1Y5KIS6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B1748_02455 {ECO:0000313|EMBL:OUS78475.1};
OS Paenibacillus sp. MY03.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS78475.1, ECO:0000313|Proteomes:UP000195591};
RN [1] {ECO:0000313|EMBL:OUS78475.1, ECO:0000313|Proteomes:UP000195591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY03 {ECO:0000313|EMBL:OUS78475.1,
RC ECO:0000313|Proteomes:UP000195591};
RA Liu H., Cheng Y., Gu J.Y., Han W.J.;
RT "Draft genome of a polysaccharide-degrading bacterium Paenibacillus sp.
RT MY03.";
RL Submitted (MAR-2017) 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}.
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:OUS78475.1}.
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DR EMBL; MXQD01000002; OUS78475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5KIS6; -.
DR OrthoDB; 9765625at2; -.
DR Proteomes; UP000195591; Unassembled WGS sequence.
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; 3.10.20.300; mk0293 like domain; 1.
DR Gene3D; 3.30.70.1380; Transcriptional regulatory protein pf0864 domain like; 1.
DR HAMAP; MF_01074; LarC; 1.
DR InterPro; IPR002395; Kininogen.
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.
DR PRINTS; PR00334; KININOGEN.
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:UP000195591}.
FT REGION 68..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 56522 MW; B5F51F4445985A26 CRC64;
MKTLYLDCVS GIAGDMTLSA LVDLGADAAY ISEQLRTLPI DEFTMAFVPV IRKGISAKWL
DLRFEESQDG HGHSHSHEHG HDHGHSHSHG HSHAHDHGHS HSHEHSHSHD HGHLHSHEHA
HDHGHSHSHD HGHDHDHGHS HSHEHGHHHG HNHSHSHDHS HSHDHGHSHS HEHGHDHSHT
HDHHHDHEHR KASDILAMIR NSALPARVKA RCLAIFEVIA EAEAKIHGMS PADVHFHEVG
AMDSIVDIIG VCLALENLGI DRIVVSPVPV GHGRIRIAHG VYPIPAPATA EIMTGVPISA
FTAQGELTTP TGAGIVKALA SSFGPTPAGV VERIGYGAGT KDMDHPNVVR AVLYREENAA
QSERILVLET QVDDMTGERL GYTMERLFGA GALDVYYTPV FMKKNRPGVL LTVLCHTRDK
AACEDILLLE TSTFGVRSYE ADRRILDRSW VEAETRYGMI KVKQAHDGER LVKSSPEYED
AAKAARKYGV SLEEVYQEVF QSLLFRDKQG E
//
