ID A0A2V4MNJ0_9RHOB Unreviewed; 539 AA.
AC A0A2V4MNJ0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:PYC48301.1};
GN ORFNames=DI396_04705 {ECO:0000313|EMBL:PYC48301.1};
OS Litorivita pollutaquae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Litorivita.
OX NCBI_TaxID=2200892 {ECO:0000313|EMBL:PYC48301.1, ECO:0000313|Proteomes:UP000248012};
RN [1] {ECO:0000313|EMBL:PYC48301.1, ECO:0000313|Proteomes:UP000248012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSX-11 {ECO:0000313|EMBL:PYC48301.1,
RC ECO:0000313|Proteomes:UP000248012};
RA Hetharua B.H., Min D., Liao H., Tian Y.;
RT "Oceanovita maritima gen. nov., sp. nov., a marine bacterium in the family
RT Rhodobacteraceae isolated from surface seawater of Lundu port Xiamen,
RT China.";
RL Submitted (MAY-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:PYC48301.1}.
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DR EMBL; QFVT01000003; PYC48301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4MNJ0; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000248012; 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:UP000248012};
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..539
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016070688"
FT DOMAIN 50..186
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 213..269
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 299..460
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 539 AA; 59858 MW; 025332EC11479F48 CRC64;
MSLAYRGGAI RSFFAIMAMV LGLLTHAAPA TAQVTAFKQA IAESASNDRD LAAFYKANDY
KPLWIGSGGR FSNRRNALFR AIKSADDHGL PGSRYKGDEL KALVKTAKSP RDRGRLEVEF
SRRFLDLATS MQTGTLVPKR VISEIKRDVP LRDRSSYLVN FAKSSPAGFF RALPPKSPEY
TRLMKAKMTL ERQLGKGGWG PTVPAKSLKP GASGPAVVAL RNRLIAMGYL RRSASQTYDA
DLQKAVQRFQ GDNGLSADGV AGAGTMAELN KGVDDRLRAV IVAMERERWM NLPQGRGKRH
ILVNLTDFTA RIIDNNRETF RTRSVIGATD RDRRSPEFSD VMEFMVINPT WNVPRSITVK
EYLPMLKRNP NAAGHLRIVD ARGRTVSRSA VNFNSYTAKT FPFNLKQPPS DGNALGLVKF
MFPNKYNIYL HDTPSKSLFN REVRAFSHGC IRLADPFDFA YALLAKQTND PKGVFHAHLK
TGQESVVPLE EPVPVHLIYR TAFTTAKGGV EYRRDIYGRD ATIWKALARE GVALRAVGG
//
