ID   A0A0K1EAB8_CHOCO        Unreviewed;       569 AA.
AC   A0A0K1EAB8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Piccolo protein {ECO:0000313|EMBL:AKT37826.1};
GN   ORFNames=CMC5_019690 {ECO:0000313|EMBL:AKT37826.1};
OS   Chondromyces crocatus.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC   Chondromyces.
OX   NCBI_TaxID=52 {ECO:0000313|EMBL:AKT37826.1, ECO:0000313|Proteomes:UP000067626};
RN   [1] {ECO:0000313|EMBL:AKT37826.1, ECO:0000313|Proteomes:UP000067626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cm c5 {ECO:0000313|EMBL:AKT37826.1,
RC   ECO:0000313|Proteomes:UP000067626};
RA   Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT   "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT   high potential for natural compound synthesis and the genetic basis for the
RT   loss of fruiting body formation.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; CP012159; AKT37826.1; -; Genomic_DNA.
DR   RefSeq; WP_050430141.1; NZ_CP012159.1.
DR   AlphaFoldDB; A0A0K1EAB8; -.
DR   STRING; 52.CMC5_019690; -.
DR   KEGG; ccro:CMC5_019690; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000067626; Chromosome.
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:SF2; SLL0670 PROTEIN; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000067626};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..569
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005459152"
FT   DOMAIN          419..541
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          53..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   569 AA;  60111 MW;  CFF3D818C966CB51 CRC64;
     MSLRSVVVLL PFVPAFACGS ALEGEGGAVA PRTARVAKVE PAGATEGAAV EGVRGAVASS
     SQAGERSSDV GGGAGGAAER TGDEATSAGH QATPRSEERE ASTGTPAAAP VDDRPRLTSQ
     GYVTWIWPTP ARGDKYLGYV RNGGSVALRS TEAVRGQGCP GGYLPVEPRG YVCVDRTVTL
     APASRSVAIA EATQGKVGAF PYRYALSNGA PMYNRIPSRA EQARFEAKFG KVGSFRPLPK
     TLSGHEALAV VEPIPATDGL PEFLSGGQGL SDRMGLVRQD IPLGSMVSFT RVFEAEGRAW
     LMSADNTLVP ADRVRPFKPS TFQGVRLGGE VKLPIAWFRK EARPRWRATA GGGLEAAGGS
     FEVRTFVQLT GQRVERGGRV FLETRERDAG GAALFVAEDD ATVVEAREKL PGGVAEGQKW
     IHVRVTQGTL TAYVGNTPVF ATLMSPGAGG VSVPGRDPVK DSTTPRGTFY VTFKDRAATM
     SPEKGENRSF WIADVPHTQY FNPPFALHAA YWHERFGEPT SAGCVNVSPI DAEWLFGWSD
     PQVPEGWQGV TGAGATKENG PTTAIVVHR
//