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SAP_MYCTU
ID   SAP_MYCTU               Reviewed;         237 AA.
AC   O07802; F2GDI0; I6YD44; Q7D4T3;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Sulfolipid-1 exporter Sap {ECO:0000305};
DE   AltName: Full=Sulfolipid-1-addressing protein {ECO:0000303|PubMed:22194604};
GN   Name=sap {ECO:0000303|PubMed:22194604};
GN   OrderedLocusNames=Rv3821 {ECO:0000312|EMBL:CCP46650.1},
GN   RVBD_3821 {ECO:0000312|EMBL:AFN51847.1};
GN   ORFNames=LH57_20825 {ECO:0000312|EMBL:AIR16615.1},
GN   P425_03979 {ECO:0000312|EMBL:KBJ24898.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RG   The Broad Institute Genome Sequencing Platform;
RA   Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA   Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA   Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA   Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA   Monaco A., King S., Sohrabi A.;
RT   "Phylogenetic analysis of Mycobacterial species using whole genome
RT   sequences.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION IN TRANSPORT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=22194604; DOI=10.1074/jbc.m111.315473;
RA   Seeliger J.C., Holsclaw C.M., Schelle M.W., Botyanszki Z., Gilmore S.A.,
RA   Tully S.E., Niederweis M., Cravatt B.F., Leary J.A., Bertozzi C.R.;
RT   "Elucidation and chemical modulation of sulfolipid-1 biosynthesis in
RT   Mycobacterium tuberculosis.";
RL   J. Biol. Chem. 287:7990-8000(2012).
CC   -!- FUNCTION: Required for the transport across the inner membrane of
CC       sulfolipid-1 (SL-1), which is a major cell wall lipid of pathogenic
CC       mycobacteria. Could also transport SL1278 (2-palmitoyl-3-(C43)-
CC       phthioceranyl-alpha, alpha'-D-trehalose-2'-sulfate), which is the
CC       precursor of SL-1. May potentiate SL-1 levels and confer specificity
CC       for sulfolipids over structurally similar glycolipids.
CC       {ECO:0000269|PubMed:22194604}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:22194604}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Accumulates the precursor SL1278. Can produce SL-
CC       1, albeit at reduced levels. {ECO:0000269|PubMed:22194604}.
CC   -!- SIMILARITY: Belongs to the peptidoglycolipid addressing protein (GAP)
CC       (TC 2.A.116) family. {ECO:0000305}.
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DR   EMBL; CP003248; AFN51847.1; -; Genomic_DNA.
DR   EMBL; CP009480; AIR16615.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP46650.1; -; Genomic_DNA.
DR   EMBL; JLDD01000048; KBJ24898.1; -; Genomic_DNA.
DR   RefSeq; NP_218338.1; NC_000962.3.
DR   RefSeq; WP_003420848.1; NZ_NVQJ01000022.1.
DR   AlphaFoldDB; O07802; -.
DR   STRING; 83332.Rv3821; -.
DR   TCDB; 2.A.116.1.2; the peptidoglycolipid addressing protein (gap) family.
DR   PaxDb; O07802; -.
DR   PRIDE; O07802; -.
DR   DNASU; 886141; -.
DR   GeneID; 886141; -.
DR   KEGG; mtu:Rv3821; -.
DR   KEGG; mtv:RVBD_3821; -.
DR   PATRIC; fig|83332.111.peg.4247; -.
DR   TubercuList; Rv3821; -.
DR   eggNOG; ENOG5033YWV; Bacteria.
DR   HOGENOM; CLU_068662_0_0_11; -.
DR   OMA; VSFEPFR; -.
DR   PhylomeDB; O07802; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR021315; Gap/Sap.
DR   Pfam; PF11139; SfLAP; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Cell wall biogenesis/degradation;
KW   Lipid transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..237
FT                   /note="Sulfolipid-1 exporter Sap"
FT                   /id="PRO_0000432808"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   237 AA;  24627 MW;  DD2F9721F816A562 CRC64;
     MWSTVLVLAL SVICEPVRIG LVVLMLNRRR PLLHLLTFLC GGYTMAGGVA MVTLVVLGAT
     PLAGHFSVAE VQIGTGLIAL LIAFALTTNV IGKHVRRATH ARVGDDGGRV LRESVPPSGA
     HKLAVRARCF LQGDSLYVAG VSGLGAALPS ANYMGAMAAI LASGATPATQ ALAVVTFNVV
     AFTVAEVPLV SYLAAPRKTR AFMAALQSWL RSRSRRDAAL LVAAGGCLML TLGLSNL
 
 
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