ID A0A0Q0ICE9_9GAMM Unreviewed; 438 AA.
AC A0A0Q0ICE9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:KPZ57515.1};
GN ORFNames=AN393_00766 {ECO:0000313|EMBL:KPZ57515.1};
OS Pseudoalteromonas sp. P1-25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1723758 {ECO:0000313|EMBL:KPZ57515.1, ECO:0000313|Proteomes:UP000050552};
RN [1] {ECO:0000313|EMBL:KPZ57515.1, ECO:0000313|Proteomes:UP000050552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-25 {ECO:0000313|EMBL:KPZ57515.1,
RC ECO:0000313|Proteomes:UP000050552};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) 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:KPZ57515.1}.
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DR EMBL; LKDW01000003; KPZ57515.1; -; Genomic_DNA.
DR RefSeq; WP_055017362.1; NZ_LKDW01000003.1.
DR AlphaFoldDB; A0A0Q0ICE9; -.
DR PATRIC; fig|1723758.3.peg.776; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000050552; 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 Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR41533; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR PANTHER; PTHR41533:SF1; L,D-TRANSPEPTIDASE YCBB-RELATED; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..438
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006181209"
FT DOMAIN 134..167
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 195..358
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 438 AA; 49772 MW; 70AD0D0D6D92E734 CRC64;
MKGLFSNQVS KKVKSITLST AFIGGACISS LPALAASELE STALAGSSLI TYSSQQHLKS
NQNYYFDQNA AQLIERTEKA INWYKEIVSN GGFIPLQISE LLELGSTGKE VNLLAERLYQ
ERDLKNNACT DAECTFDQQI EQAVKQFQRR HGLKVDGRVG KRTVAKLNVP AKVKLNKLKL
NLYRITNFAG SSDEQYVYVN IPEYTLRYVK AGEVKLQNNV IVGKPSWKTP AFSDEIEKFV
VNPEWRIPTS IATKEIAPKV ARDPHYLAKN NIEVRKNSYL DSKTVNPSNI DWQAIKPYQF
DHFLVKRAGD ENPLGEVKYL FPNPEAIYVH DTPAKQRFGQ TQRALSHGCI RVEKPFSLAR
EIIKHQGETH TLKQMDEARV NDTTQTFHLD EPLPIHLVYW TAWVDEDMLV NFRDDIYQHD
TKALLNDEEQ SVIAALIK
//
