ID   A0A285ZSS3_9SPHI        Unreviewed;       511 AA.
AC   A0A285ZSS3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=L,D-transpeptidase catalytic domain {ECO:0000313|EMBL:SOD12704.1};
GN   ORFNames=SAMN06297358_0805 {ECO:0000313|EMBL:SOD12704.1};
OS   Pedobacter xixiisoli.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1476464 {ECO:0000313|EMBL:SOD12704.1, ECO:0000313|Proteomes:UP000219281};
RN   [1] {ECO:0000313|EMBL:SOD12704.1, ECO:0000313|Proteomes:UP000219281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12803 {ECO:0000313|EMBL:SOD12704.1,
RC   ECO:0000313|Proteomes:UP000219281};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; OCMT01000001; SOD12704.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285ZSS3; -.
DR   OrthoDB; 9778545at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000219281; 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; IPR045380; LD_TPept_scaffold_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR41533:SF2; BLR7131 PROTEIN; 1.
DR   PANTHER; PTHR41533; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR   Pfam; PF20142; Scaffold; 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   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        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          77..222
FT                   /note="L,D-transpeptidase scaffold"
FT                   /evidence="ECO:0000259|Pfam:PF20142"
FT   DOMAIN          256..442
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   511 AA;  58005 MW;  EEF79302561AFD7E CRC64;
     MNTHRTSING LSIFIVALLI IIIGFSACKK SESEVGKLAF KVSGNKIFKE INDEAFAEKL
     KTVSKEKSMD FKNPKFLTAF YEKHNYAPVL LTKILKDNQL DSVVSVLNRV DAHGLSSKLF
     DGEQIKSTYE KIAHKNKISD LGEAYSVLVD LELSLANAIT NYSNAMQFGV VSPRRIYAQY
     YTKTKRPDEK SFFEALEAID PTKFLDSVQP KDKQYVALQK ALKSQRTSTS AGGEEAERIL
     IVNLERLRWQ NKPSEDKYVW VNIPDFSLDV IEDEKSTLRM KVCVGEGRNQ DYKDKLIEYD
     ESGLKKDRPF NRETPQLSSL IHSVQVNPVW NIPESIANNE ITKYAAADPY YLANNNIDVY
     LNGKKVEDPE TVNWAVDGAG KKYKFKQRPG EDNSLGKIKF LFDNQSSVYL HDTPNQQAFN
     QQVRAVSHGC VRVEKPLELA QALFGNGATY EGIKKAMQTG EPKVNDIALK NKVPVYLSYL
     TCWQDDTGKL QYRKDVYGLD IVLYTHLIRL K
//