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
//