ID A0A2I1DNA3_9PROT Unreviewed; 334 AA.
AC A0A2I1DNA3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=L,D-transpeptidase {ECO:0000313|EMBL:PKY11347.1};
GN ORFNames=B1757_05005 {ECO:0000313|EMBL:PKY11347.1};
OS Acidithiobacillus marinus.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=187490 {ECO:0000313|EMBL:PKY11347.1, ECO:0000313|Proteomes:UP000234329};
RN [1] {ECO:0000313|EMBL:PKY11347.1, ECO:0000313|Proteomes:UP000234329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH {ECO:0000313|EMBL:PKY11347.1,
RC ECO:0000313|Proteomes:UP000234329};
RA Sharmin S., Tokuhisa M., Kanao T., Kamimura K.;
RT "Draft genime sequence of the acidophilic sulfur-oxidizing bacterium
RT Acidithiobacillus sp. SH, isolated from seawater.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the YkuD family.
CC {ECO:0000256|ARBA:ARBA00005992}.
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:PKY11347.1}.
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DR EMBL; MXAV01000017; PKY11347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1DNA3; -.
DR InParanoid; A0A2I1DNA3; -.
DR OrthoDB; 463216at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000234329; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000234329};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 150..279
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 334 AA; 37803 MW; 277D8C65B04B25AF CRC64;
MHMLIPTAPT AATLSSSTQE LLHAREIRKI LIKLRYLPLI PVDYLGLHGH IHGSYQWRFK
IPRALQTLAA SDSWQDPWNP LVLGALYQFE AVHHLPVEPG DMGIRGLPPT IEKALVHAKK
NDPDPWTWIL VTKFPRPEEI HLFMGGHGWI FQSKANTGVM HATPDGTWPV YARDTHTAMI
GRFPIPVPKA QVRLYEAAKS AGYALQSVHY ARYHHHWVQY QHYDDPDIRW VNYFDRGRAV
HFYPRASYGF PQSAGCVELP KSAAHKIYAL IHYGTPVTVS HSAVGPWDPP GSAYLDAPQK
SQQLHLTYQE IPSKSSPRSV HLQLVETAVK RPTS
//