ID A0A0H3GQE8_KLEPH Unreviewed; 313 AA.
AC A0A0H3GQE8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=L,D-transpeptidase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=KPHS_34570 {ECO:0000313|EMBL:AEW62155.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW62155.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW62155.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW62155.1,
RC ECO:0000313|Proteomes:UP000007841};
RX PubMed=22408243; DOI=10.1128/JB.00043-12;
RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA Ou H.Y.;
RT "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT HS11286, a multidrug-resistant strain isolated from human sputum.";
RL J. Bacteriol. 194:1841-1842(2012).
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; CP003200; AEW62155.1; -; Genomic_DNA.
DR RefSeq; WP_014343266.1; NC_016845.1.
DR RefSeq; YP_005227757.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GQE8; -.
DR STRING; 1125630.KPHS_34570; -.
DR GeneID; 11848485; -.
DR KEGG; kpm:KPHS_34570; -.
DR PATRIC; fig|1125630.4.peg.3368; -.
DR HOGENOM; CLU_046834_0_1_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007841; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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 InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR041597; Ldt_C.
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; PF17969; Ldt_C; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000007841};
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..313
FT /note="L,D-transpeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002610401"
FT DOMAIN 99..231
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT DOMAIN 236..304
FT /note="L,D-transpeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17969"
SQ SEQUENCE 313 AA; 34158 MW; 3AD83EDE686599BE CRC64;
MTMRRVKLVC SALMLLASHG ALAVSYPLPP EGSRLVGSAF TIAVPDNNTQ PLESFAAQYG
QGLSNMLEAN PGVDVYLPRS GSTLTIPQQL ILPDTVREGI VINVAEMRLY YYPPLGNSVE
VLPIGIGQAG RETPRNWVTA VERKQEGPTW VPTANTRREY AKEGKTLPAM VPPGPDNPMG
LYAIYIGRLY AIHGTNANFG IGLRVSQGCI RLRNDDIKFL FDNVPVGTRV QLIDQPVKYS
VEPDGSHWLE VHEPLSRNRA EFESDRKVPL PMTSALRDFT QGPGVSPAQV EQTLQRRSGM
PVNISATAAQ GSL
//
