ID A0A0W0Z114_9GAMM Unreviewed; 185 AA.
AC A0A0W0Z114;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Enhanced entry protein EnhA {ECO:0000313|EMBL:KTD62836.1};
GN Name=enhA_2 {ECO:0000313|EMBL:KTD62836.1};
GN ORFNames=Lsha_0868 {ECO:0000313|EMBL:KTD62836.1};
OS Legionella shakespearei DSM 23087.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD62836.1, ECO:0000313|Proteomes:UP000054600};
RN [1] {ECO:0000313|EMBL:KTD62836.1, ECO:0000313|Proteomes:UP000054600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD62836.1,
RC ECO:0000313|Proteomes:UP000054600};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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:KTD62836.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNYW01000029; KTD62836.1; -; Genomic_DNA.
DR RefSeq; WP_018577449.1; NZ_LNYW01000029.1.
DR AlphaFoldDB; A0A0W0Z114; -.
DR STRING; 1122169.Lsha_0868; -.
DR PATRIC; fig|1122169.6.peg.1006; -.
DR eggNOG; COG1376; Bacteria.
DR OrthoDB; 463216at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000054600; Unassembled WGS sequence.
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; 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; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF34; L,D-TRANSPEPTIDASE YCIB-RELATED; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..185
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006918186"
FT DOMAIN 62..182
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 185 AA; 19968 MW; 09DAA0EC8DA44FB8 CRC64;
MKKQLLLVPV CALAASCASM DRSTAVVDDA GYTHYTMSMA SDHKGANYFP EKREATGRKV
FIFDPKATAW AAYDAQGNRV NTGSASGGKD FCEDVGRGCR TVTGSFKVYS KKGEECTSSI
YPIETGGGAK MPYCMHFSGG YSIHAAYEVP NYNASHGCIR VLPSAAKWLN QNFIDIGTSV
IVKPY
//
