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HEPA_NOSS1
ID   HEPA_NOSS1              Reviewed;         607 AA.
AC   P22638;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 3.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Heterocyst differentiation ATP-binding protein HepA;
GN   Name=hepA; Synonyms=hetA; OrderedLocusNames=alr2835;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2111805; DOI=10.1128/jb.172.6.3131-3137.1990;
RA   Holland D., Wolk C.P.;
RT   "Identification and characterization of hetA, a gene that acts early in the
RT   process of morphological differentiation of heterocysts.";
RL   J. Bacteriol. 172:3131-3137(1990).
RN   [2]
RP   SEQUENCE REVISION.
RA   Zhu J., Wolk C.P.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- FUNCTION: Acts early in the process of morphological differentiation of
CC       heterocysts.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- INDUCTION: By deprivation of nitrate.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC32400.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF031959; AAC32400.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000019; BAB74534.1; -; Genomic_DNA.
DR   PIR; AD2160; AD2160.
DR   RefSeq; WP_010996986.1; NZ_RSCN01000003.1.
DR   AlphaFoldDB; P22638; -.
DR   SMR; P22638; -.
DR   STRING; 103690.17131929; -.
DR   EnsemblBacteria; BAB74534; BAB74534; BAB74534.
DR   KEGG; ana:alr2835; -.
DR   eggNOG; COG1132; Bacteria.
DR   OMA; PIMNLGF; -.
DR   OrthoDB; 643917at2; -.
DR   Proteomes; UP000002483; 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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043158; P:heterocyst differentiation; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Heterocyst; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..607
FT                   /note="Heterocyst differentiation ATP-binding protein HepA"
FT                   /id="PRO_0000092339"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        163..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        186..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          32..330
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          364..598
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         397..404
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   607 AA;  67790 MW;  B47970D4758F564F CRC64;
     MPKSPHKLFK ANSFWKENNL ILREIKHFRK IAILAVIFSF LAASFEGVSI GFLLSFLQKL
     TSPNDPIQTG ISWVDMILAA DAWPIPPIYR ISLLILLSTW MRATFNYFGG VYTESAQLNL
     ADRLHKQIFE QLQALRLSYF AQTRSGELIN TITTEIERIK QGFSGLAFVL TRIMTVCVYF
     VVMFSISWQL SIISVLIFLL LAVGLSTLNK RVRETSFGIS HANAQFTAVA VEFINGIRTI
     QAFGTQEFER QRFYKASTNQ LNAAIKVVLA WTLVKPIAEG IATTVLISLI VISFATFTLP
     VASLLTFFFV LVRVIPNIQD INGTVAFLST LQGSSENIKN ILQTNNKPYL KNGKLHFQGL
     KRSIDLVSVD FGYTADNLVL NNITLTIERG KTTALVGASG AGKTTLADLI PRFYDPTEGQ
     ILVDGLDVQY FEINSLRRKM AVVSQDTFIF NTSIRDNIAY GTSGASEAEI REVARLANAL
     QFIEEMPEGF DTKLGDRGVR LSGGQRQRIA IARALLRDPE ILILDEATSA LDSVSERLIQ
     ESIEKLSVGR TVIAIAHRLS TIAKADKVVV MEQGRIVEQG NYQELLEQRG KLWKYHQMQH
     ESGQTNS
 
 
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