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Database: UniProt
Entry: C1DBU5_LARHH
LinkDB: C1DBU5_LARHH
Original site: C1DBU5_LARHH 
ID   C1DBU5_LARHH            Unreviewed;       218 AA.
AC   C1DBU5;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=ErfK/YbiS/YcfS/YnhG family protein {ECO:0000313|EMBL:ACO75498.1};
GN   OrderedLocusNames=LHK_02516 {ECO:0000313|EMBL:ACO75498.1};
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Laribacter.
OX   NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO75498.1, ECO:0000313|Proteomes:UP000002010};
RN   [1] {ECO:0000313|EMBL:ACO75498.1, ECO:0000313|Proteomes:UP000002010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9 {ECO:0000313|EMBL:ACO75498.1,
RC   ECO:0000313|Proteomes:UP000002010};
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA   Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA   Pallen M.J., Lok S., Yuen K.Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the YkuD family.
CC       {ECO:0000256|ARBA:ARBA00005992}.
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DR   EMBL; CP001154; ACO75498.1; -; Genomic_DNA.
DR   RefSeq; WP_012697984.1; NC_012559.1.
DR   AlphaFoldDB; C1DBU5; -.
DR   STRING; 557598.LHK_02516; -.
DR   KEGG; lhk:LHK_02516; -.
DR   eggNOG; COG1376; Bacteria.
DR   HOGENOM; CLU_042399_3_0_4; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002010; Chromosome.
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:SF24; L,D-TRANSPEPTIDASE ERFK_SRFK-RELATED; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002010};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..218
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002908564"
FT   DOMAIN          53..214
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   218 AA;  23662 MW;  E56E557C254C65FE CRC64;
     MMKLLTLLWA CLLAAPALAS SSPAPSRLAG FVLDQQSSSL LPGQTNPRHP GEPWIRVGVG
     SQTLTLFDGD GTPRRHWVIS TAKNGVGEQF GSYQTPRGWH TVCDKIGADA APDAIFYRRQ
     DTGWRYSAEL ARENPDKDWI LTRILWLCGA EPGFNQGELP DGTLVDSYQR GIYIHGGGAH
     VPFGTPTSKG CVRMTTPSVI DLFELVPTGT DVWIDVAG
//
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