ID A0A1N6SYS6_9GAMM Unreviewed; 319 AA.
AC A0A1N6SYS6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=L,D-transpeptidase YbiS {ECO:0000313|EMBL:SIQ46251.1};
GN ORFNames=SAMN05880558_103335 {ECO:0000313|EMBL:SIQ46251.1};
OS Aeromonas sp. RU39B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1907416 {ECO:0000313|EMBL:SIQ46251.1, ECO:0000313|Proteomes:UP000186911};
RN [1] {ECO:0000313|EMBL:SIQ46251.1, ECO:0000313|Proteomes:UP000186911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU39B {ECO:0000313|EMBL:SIQ46251.1,
RC ECO:0000313|Proteomes:UP000186911};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the YkuD family.
CC {ECO:0000256|ARBA:ARBA00005992}.
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DR EMBL; FTMJ01000003; SIQ46251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6SYS6; -.
DR STRING; 1907416.SAMN05880558_103335; -.
DR InParanoid; A0A1N6SYS6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000186911; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; cd00118; LysM; 1.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR041597; Ldt_C.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF32; L,D-TRANSPEPTIDASE ERFK/SRFK-RELATED; 1.
DR Pfam; PF17969; Ldt_C; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF03734; YkuD; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..319
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013383207"
FT DOMAIN 40..85
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 319 AA; 35342 MW; 781B43753A5DF11B CRC64;
MMKSWQSLAL LTGLLCKVLP AAAIEYALPT EGSRLIGKNI EYVVPNDGHS LEQIAAQFQL
GLTNLLEANP GVDPYLPRPG SKLVIPHQLL LPDTVHEGII INLAEMRLYY YPKGEKKVHV
LPIGIGQLGA GTPENWVTKV ERKRANPTWT PTENIRRRYA ARGETLPAVW PAGPDNPMGL
FALYIGNLYA IHGTNANFGI GLRVSSGCVR LRNDDIEFLF KKVPVGTRVQ FINQPVKKSL
EPDGSRYLEV HQPLSRSEEE YKSNGIVPLP MTPALTRFIA SKETNSKVVK QALEQRTGIP
MRINNKAATG EPVNHDELF
//