ID A1BIC0_CHLPD Unreviewed; 563 AA.
AC A1BIC0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Peptidoglycan-binding domain 1 protein {ECO:0000313|EMBL:ABL66147.1};
GN OrderedLocusNames=Cpha266_2142 {ECO:0000313|EMBL:ABL66147.1};
OS Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL66147.1, ECO:0000313|Proteomes:UP000008701};
RN [1] {ECO:0000313|EMBL:ABL66147.1, ECO:0000313|Proteomes:UP000008701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266 {ECO:0000313|EMBL:ABL66147.1,
RC ECO:0000313|Proteomes:UP000008701};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; CP000492; ABL66147.1; -; Genomic_DNA.
DR RefSeq; WP_011745946.1; NC_008639.1.
DR AlphaFoldDB; A1BIC0; -.
DR STRING; 290317.Cpha266_2142; -.
DR KEGG; cph:Cpha266_2142; -.
DR eggNOG; COG2989; Bacteria.
DR HOGENOM; CLU_020360_3_4_10; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008701; 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:UP000008701};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 73..209
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 236..294
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 322..488
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 563 AA; 64158 MW; D68F29DE2DD1D3FE CRC64;
MPFISIITYF LVCLAFSPVK QESRQQLQSD SSAQALQTKK TDLSPVAEQI RCHFEKVQGI
APSDAVRQTF NNRLALFYTA REFKPVWTKQ TMAAELISAI DKAEQHGLIP ADYHSTEIRY
FSENPPLTPQ LQARYDLLLS DAFLTLAYHL RFGKVLPESL DPDWNVNRTL AKSALEFRLQ
QAIAAERIAG LLDELSPRHP GYERMKKGLA HYRVIVKTGG WQKVTEGKKI KEGDRDNRVR
QIRRRLQESG DLVFRSADTS RVFSKAMADA VVRFQKRNGL SVDGAAGAET IREMNISAAE
RIEQIRINME RYRWFIGDLE QRAVLVNIPG FTLQYIDNGQ PRWETRVIVG KTGRETPLFK
ADMQYIVFNP QWVIPPTILA KDALPGIRKS RSYLYSRNLK VIDRNGRVVD PATVNWSQYT
AANLPYRLQQ TAGDHGSLGR IKFMLPNKHI VYLHDTPHKE LFQKSTRNFS SGCIRVQNPL
ELAELVLQDS VKWNSDAINA AIKTGKTSNV NLPKHIPVYL LYLTAFPQDD AIHFRGDVYN
RDNDVLKALN KSLPEFKTES CGL
//
