ID A0A0F2P1X6_9GAMM Unreviewed; 575 AA.
AC A0A0F2P1X6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Peptidoglycan-binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VR73_06355 {ECO:0000313|EMBL:KJS08278.1};
OS Gammaproteobacteria bacterium BRH_c0.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1629722 {ECO:0000313|EMBL:KJS08278.1, ECO:0000313|Proteomes:UP000033581};
RN [1] {ECO:0000313|EMBL:KJS08278.1, ECO:0000313|Proteomes:UP000033581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c0 {ECO:0000313|EMBL:KJS08278.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-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:KJS08278.1}.
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DR EMBL; LADM01000050; KJS08278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2P1X6; -.
DR STRING; 1629722.VR73_06355; -.
DR PATRIC; fig|1629722.3.peg.149; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000033581; 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 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 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..575
FT /note="Peptidoglycan-binding protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002456265"
FT DOMAIN 58..210
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 286..318
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 347..499
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 575 AA; 63904 MW; 448506EFB089A913 CRC64;
MWCGVWTLLA VAVSAGISSA SAVTVASDPS SSLQRQLANP APACVISAVD DDHPVARTVA
GLYADNDFRP LWLDSQRYES LILAIDGLVE DGLDPLDYGV MQLRELRDIA VTDHDALVCR
ELQASYGYLN ALYHLSHGKL NAEALEPLWR APRADGALTE VAPLVGLEHQ AQLDTLAQLE
SLAASGLADI GVAFQRARPG LARYHQLRQA YGQWRDQYRF VGWPQVPPGP ILRPGMEDSR
TPLVRQRLEA EGYLSPAGGE MAGREMAAPE VAAPEVASPE VASAEQYDET LSAAVREFQR
RHRLKTDGIV GPQTRQEMNL SRAFRYDQIR ANLERLRWLW REIEFNTVLV DIAGAEVIYL
RDYAPLWRSR VQVGTSARPT PVLKSRITHL TFNPTWTVPP TIYRKDKLPE IRRDIGYLAK
NRIRVLGPDG RQLDPYAINW NNPGAIRLRQ DAGPNNALGL VAIRFPNPFA VYLHDTPNRK
LFANEQRTTS SGCVRVEGAM DLSSILFEGV SEDKRLQIEA IKASGRTRNV NLPTPVPIVL
AYWTVDVDED GELEFRPDIY SRDDALVNAL RAGGN
//
