ID A0A1M4XLU0_9CLOT Unreviewed; 538 AA.
AC A0A1M4XLU0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative peptidoglycan binding domain-containing protein {ECO:0000313|EMBL:SHE94401.1};
GN ORFNames=SAMN02745158_02022 {ECO:0000313|EMBL:SHE94401.1};
OS Lactonifactor longoviformis DSM 17459.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Lactonifactor.
OX NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHE94401.1, ECO:0000313|Proteomes:UP000184245};
RN [1] {ECO:0000313|EMBL:SHE94401.1, ECO:0000313|Proteomes:UP000184245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17459 {ECO:0000313|EMBL:SHE94401.1,
RC ECO:0000313|Proteomes:UP000184245};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; FQVI01000009; SHE94401.1; -; Genomic_DNA.
DR RefSeq; WP_072851281.1; NZ_FQVI01000009.1.
DR AlphaFoldDB; A0A1M4XLU0; -.
DR STRING; 1122155.SAMN02745158_02022; -.
DR OrthoDB; 3176960at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000184245; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.10.20.800; -; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR038054; LD_TPept-like_central_sf.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR InterPro; IPR022029; YoaR-like_PG-bd.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF2; SLL0670 PROTEIN; 1.
DR Pfam; PF12229; PG_binding_4; 2.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR SUPFAM; SSF143985; L,D-transpeptidase pre-catalytic domain-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000184245};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 71..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..254
FT /note="YoaR-like putative peptidoglycan binding"
FT /evidence="ECO:0000259|Pfam:PF12229"
FT DOMAIN 274..386
FT /note="YoaR-like putative peptidoglycan binding"
FT /evidence="ECO:0000259|Pfam:PF12229"
FT DOMAIN 410..534
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 39..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..67
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 60313 MW; F3535A2F38170B38 CRC64;
MSKKKKKLQE NQVEAAGAVD PRIDEAMAKI VQDTIGNDTV YDQPKKKKNR KAAKASGQKS
KMKKKKSKNT ALKVTGIVAG VVILLAGAAY GVGAYYYHDK FFKGTEINGI NCENMTVEET
EDLIRRQVED YKITVQFRGD QAQEILGSDI GYQYVSNGDA EKILKEQNPL LWIRGYFKPE
KYEAAKNISF DENQLRTKLD SLDCMIAENQ EAPQDAYVTF QETEFVIVDE VQGTTIDENT
MFEALKTAVS ESRPDVSAEE AGAYAAPSVT KDNQDLIAQR DMLNTYAKAS ITYTFGEQTE
LLDGSIIKDW FDYDENGNII ENEDTFKANA KEYVKSLAAK YDTVGKERSF HSTAAGADIT
VKGGSYGWKI NQKKEVAQLI EEIKAGTVTT REPIYSSTAV SRDGNEIGNT YVEVDLGNQH
MWFYKDGQLI VDSDFVSGNM SYKDRVTPSG VYSLYYKQRD KTLRGKKNPD GTYEYESPVK
YWMPFNGGVG LHDASWRSNF GGNIYKTSGS HGCINLPRSK AQVLYENIEK DVPIVCFY
//
