ID A0A2G1XD36_STRCJ Unreviewed; 383 AA.
AC A0A2G1XD36;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=L,D-transpeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BLA24_23955 {ECO:0000313|EMBL:PHQ49132.1}, CYQ11_22115
GN {ECO:0000313|EMBL:PPT15219.1};
OS Streptomyces cinnamoneus (Streptoverticillium cinnamoneum).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces cinnamoneus group.
OX NCBI_TaxID=53446 {ECO:0000313|EMBL:PHQ49132.1, ECO:0000313|Proteomes:UP000222531};
RN [1] {ECO:0000313|EMBL:PHQ49132.1, ECO:0000313|Proteomes:UP000222531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21532 {ECO:0000313|EMBL:PHQ49132.1,
RC ECO:0000313|Proteomes:UP000222531};
RX PubMed=29053243;
RA Patteson J., Cai W., Johnson R.A., Santa Maria K., Li B.;
RT "Identification of the Biosynthetic Pathway for the Antibiotic
RT Bicyclomycin.";
RL Biochemistry 0:0-0(2017).
RN [2] {ECO:0000313|EMBL:PPT15219.1, ECO:0000313|Proteomes:UP000239771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41675 {ECO:0000313|EMBL:PPT15219.1,
RC ECO:0000313|Proteomes:UP000239771};
RA Vior N.M., Lacret R., Chandra G., Dorai-Raj S., Trick M., Truman A.W.;
RT "Discovery and biosynthesis of the antibiotic bicyclomycin in distant
RT bacterial classes.";
RL Submitted (DEC-2017) 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:PHQ49132.1}.
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DR EMBL; NHZO01000154; PHQ49132.1; -; Genomic_DNA.
DR EMBL; PKFQ01000001; PPT15219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1XD36; -.
DR OrthoDB; 5242354at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000222531; Unassembled WGS sequence.
DR Proteomes; UP000239771; 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; cd13432; LDT_IgD_like_2; 1.
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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000222531};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..201
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 225..327
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 383 AA; 41590 MW; 4294CD838A347C43 CRC64;
MLAGCATVGP PKTALTDDAR PPAQLVHVVP HDGARNVSAA ERFEVRAPRG RLERVRVSAF
RDGIQLTVPG RISADRHRWL PADRGHLRLG ARYAVDVVAV DSSGRRTARH SGFTTYVPQH
RFIGYFTPEP QSVVGTGMIV SFGFSRPITD RAAVERAIRV TAQPPTEVAA HWFGPARLDF
RPRTYWKPGT VVTLDLKLRD VRGAEGVYGL QQKTVRFVVG RRQFSTVDAA THTMRVVRDG
KAPVTLPVTA GGPGNETYNG KMVISEKFDM TRMNGDTVGF GGEYDISDVP HAMRLTATGT
FLHGNYWAPA DAFGATNTSH GCIGLRDTQG GSLSSPAGWF FSGSLVGDVV EVVHSGDRQV
APDNGLSGWN MSWRDWRAGS ALD
//