ID G2KLS3_MICAA Unreviewed; 589 AA.
AC G2KLS3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative peptidoglycan binding domain protein {ECO:0000313|EMBL:AEP09302.1};
GN OrderedLocusNames=MICA_971 {ECO:0000313|EMBL:AEP09302.1};
OS Micavibrio aeruginosavorus (strain ARL-13).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Micavibrio.
OX NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP09302.1, ECO:0000313|Proteomes:UP000009286};
RN [1] {ECO:0000313|EMBL:AEP09302.1, ECO:0000313|Proteomes:UP000009286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARL-13 {ECO:0000313|EMBL:AEP09302.1,
RC ECO:0000313|Proteomes:UP000009286};
RX PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA Wang Z., Kadouri D., Wu M.;
RT "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT aeruginosavorus ARL-13.";
RL BMC Genomics 12:453-453(2011).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; CP002382; AEP09302.1; -; Genomic_DNA.
DR RefSeq; WP_014102525.1; NC_016026.1.
DR AlphaFoldDB; G2KLS3; -.
DR STRING; 856793.MICA_971; -.
DR KEGG; mai:MICA_971; -.
DR eggNOG; COG2989; Bacteria.
DR HOGENOM; CLU_020360_3_4_5; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000009286; 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 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:SF2; BLR7131 PROTEIN; 1.
DR PANTHER; PTHR41533; L,D-TRANSPEPTIDASE HI_1667-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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009286};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..589
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003432609"
FT DOMAIN 82..218
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 270..303
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 331..499
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 589 AA; 65507 MW; 88882F9B6FA925EF CRC64;
MSARFSRRIF KSLMIAGASV AIGIGAAQYA QAESVAGPTN PSLKMAALPF ANIGENRIIR
TEISTKLSSG SVDGRPFRNP DAMQAAYASR NGEPLWIGRS GVSDHVADFI AVLEESWTHG
LNPEQYHLTQ IKTLAGSESP QDKAHLDLLI SDAVMRYGQD VTGMRVAPDR IRQKAEYWRQ
PMAAGDVLMQ VSASDDPADT LEDLAPQGSL YDRLRDELVT LSRSPERAAE DAGPVNFGGG
LLRPGEYHKN VPVLRARMGQ THDPAYGPEN LYDDELAAAV MKFQAQHGLS ADGVLGPKTL
AFMNQSVRQK MEQIIVNLER LRWLEQEKPH RYILVNIPSA TLWAVEGNSV EAQMPVIVGR
KDRPTKSFTT EITGIRFNPK WNVPTTIKTK DYLPRLKEDP YYLQDKGIEV YRVIEGRRET
VDPASVDWAN MTRADLARLN MQQGSGDNNA LGRIRVLMPN QYDIYLHDTN SPGLFANNDR
TLSSGCVRMA DPEKVARFIL GPNPGWSDDR MHGLIARGST SEVKAEQTLP VYFLYQTVWL
DNRGQLVYGP DIYNEDQRLL AVLKDMKAYA IPDRDGVKFA AISQNPVVR
//
