ID A0A1Z2L884_9ACTN Unreviewed; 407 AA.
AC A0A1Z2L884;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Lipoprotein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SMD11_4907 {ECO:0000313|EMBL:ARZ70500.1};
OS Streptomyces albireticuli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1940 {ECO:0000313|EMBL:ARZ70500.1, ECO:0000313|Proteomes:UP000195755};
RN [1] {ECO:0000313|EMBL:ARZ70500.1, ECO:0000313|Proteomes:UP000195755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK11 {ECO:0000313|EMBL:ARZ70500.1,
RC ECO:0000313|Proteomes:UP000195755};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Yao L., Wang C.;
RT "Streptomyces albireticuli Genome sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP021744; ARZ70500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z2L884; -.
DR KEGG; salj:SMD11_4907; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000195755; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..407
FT /note="Lipoprotein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013368879"
FT DOMAIN 47..210
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 235..356
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 387..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 43190 MW; 3A33D9AF06539CDF CRC64;
MVHLCAMVVS SVALGATACG GSSNPLADAP YDATGQVALT GAEDGRKADP SKPLEVTADG
SDRITDVTAT DAAGRFVKGE LDADGRRWHS TGALAAGAHY TVRVSTEDED GFQGRRTVGF
DTSAADRLLR VAFGPQSGTY GVGQPVTAEL SAPVQDPAAR AVVERALKVD TRPAVEGAWH
WVDNRTLHYR PKDYWPARTT VAVRSGLDGI KVAGGLYGGS SKPVKLTIGD RIEAVTDAAA
HSMTVLRNGK EIRSIPVTTG KPGYATRNGV KVVLGRESFV RMRGTSIGIA EGSEDSYDLP
VRWATRVTWS GEYVHAAPWS EGSQGSENVS HGCTGMSTDN AKWFFDTIHL GDLVKVVNSA
GTTMTPFDNG FGDWNMPWKQ WREGSALAAG KRDGSNPADA ARLRPEM
//
