ID A0A3D8MTL0_9DELT Unreviewed; 813 AA.
AC A0A3D8MTL0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Murein L,D-transpeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DV096_14060 {ECO:0000313|EMBL:RDV37624.1};
OS Bradymonadaceae bacterium TMQ3.
OC Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae.
OX NCBI_TaxID=2283320 {ECO:0000313|EMBL:RDV37624.1, ECO:0000313|Proteomes:UP000256871};
RN [1] {ECO:0000313|EMBL:RDV37624.1, ECO:0000313|Proteomes:UP000256871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMQ3 {ECO:0000313|EMBL:RDV37624.1,
RC ECO:0000313|Proteomes:UP000256871};
RA Wang S.;
RT "Lujinxingia celare sp. nov., isolated from a marine island.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:RDV37624.1}.
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DR EMBL; QRGZ01000005; RDV37624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8MTL0; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000256871; Unassembled WGS sequence.
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; 2.
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; 2.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..813
FT /note="Murein L,D-transpeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017607801"
FT DOMAIN 91..156
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 368..418
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 456..537
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT DOMAIN 675..755
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 571..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 91310 MW; 2C35078B4F9B1234 CRC64;
MIFNTPHRAS HSLRLLAMGL LTSSLLAFSA CSEPTIEPAA AQSYAAQWAP TLEDALREKS
ASAAASQALK AAFEKGDEVR QASGEPPFAT LVNQLYRERE YEPALVKNAT LTPAGEALWN
ALQVIEDHQL DAAPYRLDEL ARLFEELEAK KQAYADFEGL QPTEAEIAAA TAWLTEQPVS
TFALSDDSRP QLTEALLNAP EGQRLNEALK AYETKSADVI AIEARLERLL AMGLARYARE
LRYFRLKEIF VHERHWDEYN EPDSRSTRPD AAKGPFRAGQ VWRQASHVAT EMANRRKEEI
FHRGIQQTLS DLLDAKAPQE AQAVIDRVPP QNPQYMGLIN AYRRYRDIVE AGGWQEVPTP
RSLKPGQRSE AVTHLKQRLR IEGFYPENAP IDDHYDEALE EAVREYQHTH QMVANGKPHN
VFWGSLNVPA QRRLAQIALN IKRWRSTNTR HAEDDQYVFV NIPDFNVELW KAQELKLRFG
IVVGNNNKEV NPLTGEAERA NRTPTLAAYI DRIIYNPYWN VTPRIRAESI IPKVHNHITD
AYVSRLSGLL ASAKPTPAPG ALRAPQAPTL TANRAPGMIG GPPAAAQPAA PSSAQPAAQP
TVPAAPVTAP DPAESLTTMR STDTGRVRAF KTEPLRRILE HHFPGEEGLA RFKAQFPYLD
PHTGMVDVST TNPDHIPSWY EANGYEVAFP GRTWEYVRML PGGENALGFV KIIFPNLQDI
YLHDTPHKPL FSRPVRGFSH GCIRMEQPLN MAETLLQLDG QNPDIDRILE KGDYNPIFLK
HQVPVFIEYY TVRVDDEGRP HFLADIYNYD EES
//