ID A0A095TA62_9GAMM Unreviewed; 625 AA.
AC A0A095TA62;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JAN-2026, entry version 38.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KGD73572.1};
GN ORFNames=HA49_09935 {ECO:0000313|EMBL:KGD73572.1};
OS Tatumella morbirosei.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Erwiniaceae; Tatumella.
OX NCBI_TaxID=642227 {ECO:0000313|EMBL:KGD73572.1, ECO:0000313|Proteomes:UP000029577};
RN [1] {ECO:0000313|EMBL:KGD73572.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 23360 {ECO:0000313|EMBL:KGD73572.1};
RA Smits T.H., Palmer M., Venter S.N., Duffy B., Steenkamp E.T., Chan W.Y.,
RA Coutinho T.A., Coetzee M.P., De Maayer P.;
RT "The draft genome of the Tatumella morbirosei type strain, LMG23360T
RT isolated from pineapple rot.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|PROSITE-ProRule:PRU01373}.
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:KGD73572.1}.
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DR EMBL; JPKR02000002; KGD73572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095TA62; -.
DR STRING; 642227.HA49_09935; -.
DR eggNOG; COG2989; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000029577; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
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; IPR052905; LD-transpeptidase_YkuD-like.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR045380; LD_TPept_scaffold_dom.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR NCBIfam; NF007891; PRK10594.1; 1.
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; PF20142; Scaffold; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS52029; LD_TPASE; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|PROSITE-
KW ProRule:PRU01373};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|PROSITE-ProRule:PRU01373};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW ECO:0000256|PROSITE-ProRule:PRU01373};
KW Reference proteome {ECO:0000313|Proteomes:UP000029577};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 384..565
FT /note="L,D-TPase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS52029"
FT REGION 257..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 519
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
FT ACT_SITE 538
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
SQ SEQUENCE 625 AA; 68632 MW; FC61D9B802A0D454 CRC64;
MLLTVRHKGS GMLKNGHKFR PIVLLCGLSL TLMPGASLWA AEGMTGTETH HQPANLHTSA
ESFSAITGSL PGGIHPYYLS QLAALYHARH LQPMWQDQQA VERFQQQLAE VALSGVQPQF
GQWISWLSRS DITGMQRDLI LSDAMLGYLQ FVAEAPIKGE SWLYGNTPYA LAMPPSGQIS
LWQSAVNSHR DAAFVNGLAP QHPQYLPMQD ALKKLLADHE VWPHMNGRGS VRPGDSSPEI
PVLRDILIRS GMLSENAIPS GSTPAPATHP VVISPASAST SSLQSAPAVQ QSSLVTDSTS
GTAPLADQGT VPVTPSATPV DPQTVYSPEL VDAVKRFQQW QGLAPDGVIG PRTREWLNVT
PRMRAGLLAL NMQRLRLLPD DMHNGIMVNI PNFSMSFYED GKTILRSRVI VGRPDRKTPL
MRSALNNVVL NPPWNVPTSL VREDIVPKAK SDPSYLEKHG FTLFSGWSAD SVVVNPETIN
WTMVNPATFP YRIRQSPGPQ NALGRYKFNM PSSDAIYLHD TPNHMLFQRD IRALSSGCVR
INKASELAGL LLQNVGWDGS RISGALQQGD TRFVSIRHRI PVNLYYLTAW VADDGKPQFR
TDIYNYDNLA RNGQSSVGNA GKFIL
//
