ID A0A372IGF8_9RHOB Unreviewed; 528 AA.
AC A0A372IGF8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:RFU13974.1};
GN ORFNames=DZD18_04540 {ECO:0000313|EMBL:RFU13974.1};
OS Rhodobacteraceae bacterium W635.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2303578 {ECO:0000313|EMBL:RFU13974.1, ECO:0000313|Proteomes:UP000264655};
RN [1] {ECO:0000313|EMBL:RFU13974.1, ECO:0000313|Proteomes:UP000264655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W635 {ECO:0000313|EMBL:RFU13974.1,
RC ECO:0000313|Proteomes:UP000264655};
RA Hou X.J.;
RT "Ayaqqumibacter halotolerans gen. nov., sp. nov., isolated from a saline
RT lake in Xinjiang province, China.";
RL Submitted (AUG-2018) 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:RFU13974.1}.
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DR EMBL; QVQC01000026; RFU13974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372IGF8; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000264655; 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 Reference proteome {ECO:0000313|Proteomes:UP000264655};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..528
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016648830"
FT DOMAIN 41..176
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 202..257
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 289..451
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 528 AA; 59457 MW; 3DD9ADA0616038D6 CRC64;
MSLLPVLAVL LSISVLLPAP AAAYVTAFRQ AIAEGVAQHD AMAEFYRDRD FEPIWTNEGH
ADRRQALLNA LENAAHHGLP TGRYDPDALR GAFGSAESPY ARGRAEVMAS TMFLNYANDV
QSGILDPGTV IRQIHRDPPR RDPSDLLVGF IGGDPHDFMR SLPPAHPEYL RLQRALLTFQ
RMAAEGGWGQ PVYAGRLERG DRGQSVVQLR DRLIRMGYMD RSVTAVYDAE MEAAVERFQA
NHGLLADGVA GSSTIEQINV GLETRMRQVI LAMERQRWMN WEDPDRGARH VLVNIPDYHT
YVIDNEEVTF ESRTVVGARP QDRMTPEFSD TMEHMVINPS WYVPRSITVG EYLPQMQANP
AAAGHMELLQ GGRPVSRAGV NFSQYTGNTF PFDLRQPPGP GNALGRVKFM FPNRHNIYLH
DTPSRNLFSR ETRAYSHGCV RVHRPLELAY HLLAPQEAQP RDYFHRILDS RQETQVDLVQ
PVPVHIVYWT AFVTPEGALN FRRDIYDRDT ALWAALDRAG VELPSTTS
//
