ID   A0A1I6R474_9BACL        Unreviewed;       470 AA.
AC   A0A1I6R474;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=L,D-transpeptidase catalytic domain {ECO:0000313|EMBL:SFS59424.1};
GN   ORFNames=SAMN05428962_1240 {ECO:0000313|EMBL:SFS59424.1};
OS   Paenibacillus sp. BC26.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1881032 {ECO:0000313|EMBL:SFS59424.1, ECO:0000313|Proteomes:UP000199637};
RN   [1] {ECO:0000313|EMBL:SFS59424.1, ECO:0000313|Proteomes:UP000199637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC26 {ECO:0000313|EMBL:SFS59424.1,
RC   ECO:0000313|Proteomes:UP000199637};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FPAD01000001; SFS59424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6R474; -.
DR   STRING; 1881032.SAMN05428962_1240; -.
DR   OrthoDB; 9787225at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000199637; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF24; L,D-TRANSPEPTIDASE ERFK_SRFK-RELATED; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        82..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          329..435
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          280..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  51787 MW;  560AD79A63E4D47D CRC64;
     MFEDQNDKSY LKRYVQNHPT NRMAWYLLGK QYMEEGKEAK ANYCFLQSGS VYEAYERKQH
     ELAHDPSVIL EQWNKKRRIS RLLIRISVAS VVFLGIILAA PFGMAKDEAE QDSSKETVQV
     KSPAAAKNGL RVAFIKPARE KTLGNALGAL LTGEGNASQT GLAVMLQQDG KWRKWTGETR
     ILAEAKRDGK AEAAAVRLLD GQTCDCQPGN ASSAFKAYSE WSREQEMRWT LASAIAHYHD
     RTKSWPTGMD DLTRSYPNNV LSGTSPQMKK LFPELLQAAK ERRAGKPSSG DDDSHAGKAE
     GESSDSTSAS QSTAANTSES KLSEEPLSII VDKDSHQLAV VSGDVIVRSY TVGLGGKKTP
     SGQFFISEKV KNPNGRDDGE FGSRGMTLSN TLYAIHGTDE PDSIGKDESH GCVRMNKKDL
     EELYDLVPLG TKVEIKNDVL PGAATPAAER FRLKPVQDET NTAVVYRWLT
//