ID A0A1H2ZJK1_9PSEU Unreviewed; 386 AA.
AC A0A1H2ZJK1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Lipoprotein-anchoring transpeptidase ErfK/SrfK {ECO:0000313|EMBL:SDX17545.1};
GN ORFNames=SAMN05421504_102550 {ECO:0000313|EMBL:SDX17545.1};
OS Amycolatopsis xylanica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=589385 {ECO:0000313|EMBL:SDX17545.1, ECO:0000313|Proteomes:UP000199515};
RN [1] {ECO:0000313|EMBL:SDX17545.1, ECO:0000313|Proteomes:UP000199515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 202699 {ECO:0000313|EMBL:SDX17545.1,
RC ECO:0000313|Proteomes:UP000199515};
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; FNON01000002; SDX17545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2ZJK1; -.
DR STRING; 589385.SAMN05421504_102550; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199515; 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:SDX17545.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199515};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 49..213
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 235..354
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 14..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 386 AA; 41151 MW; 20646720D6844AF1 CRC64;
MAGLVLTLAL SACSGSEPQT TNTGTGQQQS GGGQTPQAAK VTVKPAGGAQ DVAPGEPAQI
TVADGTLGSV TLTNPDGKQV KGELSADKKS WTVGEQLGYG KTYTWAGDAT GADGKKVDIS
GNFTTVKPKK QVQASINVGD GQEYGVAMPI VISFKGKVTD KQSVEKALKV ETTPKTEGSW
AWLEGDTAVH WRPKEYYKSG TTVKVEGKLY GVKIAEGTYG KEDVTADFKI GRKQVVTGNT
TEHTMQVIRE GQQIAEYPVS YGLDSDPGRV TKSGTHVVMG KQASYAMSNP RYGYENVVVP
WAVRISNNGE FIHGLAASIW AQGKKNVSHG CLNLSPKNAK EYFDGTMTGD PVEISGSTQK
LTSKDGDYSD WTYTWEEWTK LSALNS
//