ID Q4L9G7_STAHJ Unreviewed; 377 AA.
AC Q4L9G7;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE SubName: Full=CapL protein {ECO:0000313|EMBL:BAE03708.1};
GN Name=capL {ECO:0000313|EMBL:BAE03708.1};
GN OrderedLocusNames=SH0399 {ECO:0000313|EMBL:BAE03708.1};
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE03708.1, ECO:0000313|Proteomes:UP000000543};
RN [1] {ECO:0000313|EMBL:BAE03708.1, ECO:0000313|Proteomes:UP000000543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE03708.1,
RC ECO:0000313|Proteomes:UP000000543};
RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; AP006716; BAE03708.1; -; Genomic_DNA.
DR RefSeq; WP_011274725.1; NC_007168.1.
DR AlphaFoldDB; Q4L9G7; -.
DR KEGG; sha:SH0399; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_1_9; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000000543; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2}.
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 191
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 377 AA; 42022 MW; 5DE7702CF1F0BA5D CRC64;
MTTDRIFLSR PHMGGTELDY IHDAFEKNWV APLGENVTEF ENSMKNYTGV KAALALTSGT
SAIHLALIES GVKRDDIVFC SSLTFSASAN PIIYQGAKPV FIDSEKDSWN MSPIALKKAF
EKYAEKGITP KAVIAVNLYG QSAKMDEIKE ICDEYKTTLV EDAAESLGAD YKGHKSGTFG
KFGIFSFNGN KIITTSGGGM LISNDEDSIA HALFVSTQAR DKALHYQHSE LGYNYRLSNI
SAGIGRGQME VLDQRIQRRR EIFEKYDEAF GNIDGFDFQP ELPDSKSNRW LTALTIDENK
TGFSALELID ALQKNNIEAR PVWKPMHLQP YFESYDYIMV DGVDNSAHLF DHGVCLPSGS
DMTDEQQTRV IEIIKSL
//
