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Database: UniProt
Entry: A0A1Y1RLX7_9MICC
LinkDB: A0A1Y1RLX7_9MICC
Original site: A0A1Y1RLX7_9MICC 
ID   A0A1Y1RLX7_9MICC        Unreviewed;       415 AA.
AC   A0A1Y1RLX7;
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=L,D-transpeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A7979_06740 {ECO:0000313|EMBL:ORC15431.1};
OS   Rothia nasimurium.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Rothia.
OX   NCBI_TaxID=85336 {ECO:0000313|EMBL:ORC15431.1, ECO:0000313|Proteomes:UP000192359};
RN   [1] {ECO:0000313|EMBL:ORC15431.1, ECO:0000313|Proteomes:UP000192359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PT-32 {ECO:0000313|EMBL:ORC15431.1,
RC   ECO:0000313|Proteomes:UP000192359};
RA   Gaiser R.A., Van Baarlen P., Wells J.M.;
RT   "Draft genome sequence of a porcine commensal Rothia nasimurium.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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:ORC15431.1}.
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DR   EMBL; LXWF01000043; ORC15431.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1RLX7; -.
DR   OrthoDB; 5242354at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000192359; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.60.40.3710; -; 1.
DR   Gene3D; 2.60.40.3780; -; 1.
DR   Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   InterPro; IPR041280; Big_10.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF35; L,D-TRANSPEPTIDASE 2; 1.
DR   Pfam; PF17964; Big_10; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192359};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          74..234
FT                   /note="Bacterial Ig"
FT                   /evidence="ECO:0000259|Pfam:PF17964"
FT   DOMAIN          256..381
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          38..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   415 AA;  45257 MW;  354936157FB4A8A3 CRC64;
     MVKALNSETQ DAFTRRSFVT VGALGTLALA ACASEDTTAA SDPTSTSASP SPTPTPAATF
     GGAVEVYPAL DEIEVNPGEK VTVTSPDSTL TRVVVVTAEG EELPGELATD GRSWTSTENM
     LFHSHYTVSW EATDTTGAKG EGESAFSTVS AAYEVDTLIN FEDGATYGIG KIIQFNFSEP
     VVNKAEVEKS ITVTGGGDLP GKFRWYNDYM VRYRPESTWA PNSTISVTVD IFGLEMGNGM
     IGNHTTTRTF KTWNKRYALA DNNTKTIKMY VDDELVREAP ITLGNTEWPS VIGQLVIMEK
     AESYYFNPGS LNLEKDDPHY YEPFWASWTS RLTSGGVFVH QALPTAWPVV GVANVSHGCI
     GMLPEDAKFF YDTFGVGDIV ETVNTGYPQA DPDDGYGDWN IPFEHYSDSN WKGNW
//
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