ID D9VZK4_9ACTN Unreviewed; 407 AA.
AC D9VZK4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Lipoprotein {ECO:0000313|EMBL:EFL17750.1};
GN ORFNames=SSNG_05002 {ECO:0000313|EMBL:EFL17750.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL17750.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL17750.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL17750.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; GG657750; EFL17750.1; -; Genomic_DNA.
DR AlphaFoldDB; D9VZK4; -.
DR STRING; 253839.SSNG_05002; -.
DR eggNOG; COG1376; Bacteria.
DR HOGENOM; CLU_039404_3_1_11; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005763; 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:EFL17750.1};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..407
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039219246"
FT DOMAIN 68..230
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 253..381
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 42507 MW; 609B6F0629A5BBD9 CRC64;
MQPIRGRVRT GLPAVLLGAA LLLTSACSGG GNSGGSGGDN GKAGGGTAKT GTEASKAVVN
VKPDDGSKEV ATSGVLKITS SGGKLTTVTV ADTKGNAVEG KLAADGATWE PARNLAAATE
YKVHAVAKDE AGRESAKDTT FSTLTPQNTF VGHYTPEDGS TVGVGMPVSI NFTRGITNTE
AVEKAITVTA EPSVPIEGHW FGNDRLDFRP EKYWAAGTKV TVKLALDGVE GRPGVYGKQT
RTVTFTVGRS QVTTVDATSK KMEVVRDGQV LKTIPITAGA PSTTTYNGQM VISEKYKVTR
MNGATVGFGG EYDISDVPHA MRLSTSGTFV HGNYWAPSST FGSENVSHGC VGLEDERGAG
DPNTPAAWFF NESLIGDVVV VKNSKDKQIA PDNGLNGWNM DWAEWIK
//
