ID   LYSW_SULAC              Reviewed;          56 AA.
AC   Q4JAQ0;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Alpha-aminoadipate/glutamate carrier protein LysW;
DE   AltName: Full=AAA carrier protein LysW;
GN   Name=lysW; Synonyms=argW; OrderedLocusNames=Saci_0753;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [2]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RX   PubMed=23434852; DOI=10.1038/nchembio.1200;
RA   Ouchi T., Tomita T., Horie A., Yoshida A., Takahashi K., Nishida H.,
RA   Lassak K., Taka H., Mineki R., Fujimura T., Kosono S., Nishiyama C.,
RA   Masui R., Kuramitsu S., Albers S.V., Kuzuyama T., Nishiyama M.;
RT   "Lysine and arginine biosyntheses mediated by a common carrier protein in
RT   Sulfolobus.";
RL   Nat. Chem. Biol. 9:277-283(2013).
CC   -!- FUNCTION: Carrier protein that bears the covalently bound substrates
CC       for arginine and lysine biosynthesis; bound L-glutamate is sequentially
CC       converted to L-ornithine, while bound alpha-aminoadipate (AAA) is
CC       sequentially converted to L-lysine. {ECO:0000269|PubMed:23434852}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- PTM: Formation of an isopeptide bond between the gamma-carboxyl group
CC       of the C-terminal glutamate and the amino group of alpha-aminoadipate
CC       (AAA) is catalyzed by LysX. The bound AAA is then converted to L-lysine
CC       in a series of reactions catalyzed by LysZ, LysY and LysJ. Release of
CC       the product L-lysine is catalyzed by LysK. Formation of an isopeptide
CC       bond between the gamma-carboxyl group of the C-terminal glutamate and
CC       the amino group of L-glutamate is catalyzed by ArgX. The bound
CC       substrate is then sequentially converted to ornithine which is
CC       eventually converted to L-arginine (PubMed:23434852).
CC       {ECO:0000269|PubMed:23434852}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene require arginine and
CC       lysine for growth. {ECO:0000269|PubMed:23434852}.
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DR   EMBL; CP000077; AAY80129.1; -; Genomic_DNA.
DR   RefSeq; WP_011277631.1; NC_007181.1.
DR   AlphaFoldDB; Q4JAQ0; -.
DR   SMR; Q4JAQ0; -.
DR   STRING; 330779.Saci_0753; -.
DR   EnsemblBacteria; AAY80129; AAY80129; Saci_0753.
DR   GeneID; 3473284; -.
DR   KEGG; sai:Saci_0753; -.
DR   PATRIC; fig|330779.12.peg.722; -.
DR   eggNOG; arCOG01588; Archaea.
DR   HOGENOM; CLU_195720_1_0_2; -.
DR   OMA; EIVEHEC; -.
DR   UniPathway; UPA00033; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR   CDD; cd13946; LysW; 1.
DR   InterPro; IPR005906; LysW.
DR   PANTHER; PTHR40393; PTHR40393; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Isopeptide bond;
KW   Lysine biosynthesis; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..56
FT                   /note="Alpha-aminoadipate/glutamate carrier protein LysW"
FT                   /id="PRO_0000422975"
FT   ZN_FING         1..34
FT                   /note="TFIIB-type"
FT   MOTIF           50
FT                   /note="EDWGE"
FT                   /evidence="ECO:0000250"
FT   BINDING         6
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         56
FT                   /note="5-glutamyl 2-aminoadipic acid; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q976J8"
FT   MOD_RES         56
FT                   /note="5-glutamyl glutamate; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q976J8"
FT   MOD_RES         56
FT                   /note="5-glutamyl N2-lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q976J8"
FT   MOD_RES         56
FT                   /note="5-glutamyl N2-ornithine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q976J8"
SQ   SEQUENCE   56 AA;  6053 MW;  483DCC31DCB769B6 CRC64;
     MVLLKCPICG NDVNVPDDSL PGEIVEHECG AQLEVFNSNG KLALRLAEQV GEDWGE