ID A0A1G5G639_9ACTN Unreviewed; 417 AA.
AC A0A1G5G639;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Lipoprotein-anchoring transpeptidase ErfK/SrfK {ECO:0000313|EMBL:SCY46995.1};
GN ORFNames=SAMN02745898_102104 {ECO:0000313|EMBL:SCY46995.1};
OS Streptomyces sp. 136MFCol5.1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCY46995.1, ECO:0000313|Proteomes:UP000199326};
RN [1] {ECO:0000313|EMBL:SCY46995.1, ECO:0000313|Proteomes:UP000199326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCY46995.1,
RC ECO:0000313|Proteomes:UP000199326};
RA de Groot N.N.;
RL Submitted (OCT-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; FMVI01000002; SCY46995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5G639; -.
DR OrthoDB; 5242354at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199326; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13432; LDT_IgD_like_2; 1.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 2.60.40.3710; -; 1.
DR Gene3D; 2.60.40.3780; -; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR041280; Big_10.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF35; L,D-TRANSPEPTIDASE 2; 1.
DR Pfam; PF17964; Big_10; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipoprotein {ECO:0000313|EMBL:SCY46995.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199326};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 78..240
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 262..391
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 43755 MW; DEF8219D28F2D54D CRC64;
MNGQPISGTS VRTNGGRRGR GATGLLALVL GALLLLVTAC GGGDTDAGSK GKNTGGSKSE
DTTASQAVVT VAPKDGADSV ATSGALKISA DQGKLTTVKV ADPKGAEVEG KIAADGTSWE
PEQHLAAATK YSVHAVAKDS KGRQSAKDTT FTTLVPKNTF IGQYTPEDGS TVGVGMPVSI
HFTRGITDPD AVEKAIEVTA EPSVPVEGHW FGNDRLDFRP ENYWAAGTKV TVKLNLDGVE
GRPGVYGKQA KTIAFTIGRS QVSTVDASTH RMKVVRDGKE IRNIPISAGA PATTTYNGQM
VISEKLKVTR MNGDTVGFGG EYDIKDVPNA MRLSTSGTFI HGNYWGGPGV FGSTNTSHGC
VGLQDVRGGW SKTTPAAWFF NHSLIGDVVV VKKSQDKTIQ PDNGLNGWNM SWAEWTK
//
