ID A0A0K9XG78_9ACTN Unreviewed; 423 AA.
AC A0A0K9XG78;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Lipoprotein {ECO:0000313|EMBL:KNB51657.1};
GN ORFNames=AC230_15040 {ECO:0000313|EMBL:KNB51657.1};
OS Streptomyces caatingaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB51657.1, ECO:0000313|Proteomes:UP000037288};
RN [1] {ECO:0000313|Proteomes:UP000037288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT from Caatinga biome, from dry forest semiarid of Brazil.";
RL Submitted (JUL-2015) 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:KNB51657.1}.
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DR EMBL; LFXA01000009; KNB51657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9XG78; -.
DR STRING; 1678637.AC230_15040; -.
DR PATRIC; fig|1678637.3.peg.3244; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000037288; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipoprotein {ECO:0000313|EMBL:KNB51657.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037288};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..423
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005532436"
FT DOMAIN 74..235
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 258..366
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 28..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 44563 MW; BA3F0B53164B8178 CRC64;
MKDGKRRKGL AAAAAVLGGV LTLAACGGGD GDDGKGGGKD KSQSKVDAAA AQEASKAQIK
IATKTGTANA GVTADEAKVT VSDGELVSVK MTSLDEKTGK QSPVEGELAA DKKSWLPKKN
LERSTKYQIV AEAKDADGRK AVANSSFSTV SPNNSFIGSF TPEDGSTVGV GMPVSINFDK
PIKDRKAVQS HLEVTSSSGQ KVVGHWFNDQ RLDFRPQEYW KANSQVTLKM SLDKVEAAPG
IKGIQNKTVT FKIGHSQVST VDAKTHQMTV VRDGKVLKTI PISAGSPSNP TYNGQMVISE
KFKETRMDGS TVGFTKGDGK GEYDIPDVPH AMRLSTSGTF IHGSYWGGGV FGNENTSHGC
VGLKDVQGAN DPNTPGAWFF SNSQIGDVVV VKNSDDKTIA PDNGLNGWNM SWSEWVKGSA
TGA
//
