ID A0A0L0AMF6_9ENTR Unreviewed; 598 AA.
AC A0A0L0AMF6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:KNC08941.1};
GN ORFNames=AC791_09625 {ECO:0000313|EMBL:KNC08941.1};
OS Klebsiella sp. RIT-PI-d.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1681196 {ECO:0000313|EMBL:KNC08941.1, ECO:0000313|Proteomes:UP000053401};
RN [1] {ECO:0000313|Proteomes:UP000053401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-d {ECO:0000313|Proteomes:UP000053401};
RA Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-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:KNC08941.1}.
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DR EMBL; LGIT01000009; KNC08941.1; -; Genomic_DNA.
DR RefSeq; WP_049840233.1; NZ_LGIT01000009.1.
DR AlphaFoldDB; A0A0L0AMF6; -.
DR STRING; 1681196.AC791_09625; -.
DR PATRIC; fig|1681196.3.peg.723; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000053401; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
DR GO; GO:0016757; F:glycosyltransferase 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; 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 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053401};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..598
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005534020"
FT DOMAIN 94..225
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 295..331
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 359..526
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 598 AA; 65834 MW; 738E733F91B73E7B CRC64;
MLLTHNYGRR LSALSLCLAF AMAPLFSAQA DEPEVVAGDS ITAANESAQP LTQSGAIEMM
TGEQAFPENS SPQASRMAIT SMLPAGYTPV YMNALASLYA SREMKPMWED REAVKAFQQQ
LAEVAIAGFQ PQFTAWVQLL TDPAVTGMTR DVVLSDAMMG YLHFVSGIPI KGNRWLYSTK
PYTLATPPLS VINQWQMALD NGSLTHFIAI LAPQHSQYEA MHQALLALTE DRRPWPVLKA
KTSLRPGQWS NDVPALREIL VRNGMLDGGP EIVLPGDAVV SPSAETRTPA KKSTAVSAAY
DKTLVNAVKR FQSWQGLGAD GIIGGSTRDW LNVSPAQRAG LLALNIQRLR LLPDKLSTGI
MVNIPAYSLV YYQNGDPVLD SRVIVGRPDR KTPMMSSALN NVVVNPPWNV PPTLARKDIL
PKVWNDPGYL ERHGYTVMRG WNSSDAIDPW NVDWATITPS NLPFRFQQAP GAHNSLGRYK
FNMPSSDAIY LHDTPNHTLF QRDARALSSG CVRVNKASEL ANMLLTDAGW NNTRISGALK
QGDTRYVNIP QTIPVNLYYL TAFIGADGKA QYRTDIYNYD LTARSGAQII EKAEQLIR
//
