ID TAGB_DICDI Reviewed; 1906 AA.
AC P54683; Q54M83;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=Serine protease/ABC transporter B family protein tagB;
DE EC=3.4.21.-;
DE AltName: Full=Prestalk-specific protein tagB;
DE Flags: Precursor;
GN Name=tagB; ORFNames=DDB_G0286119;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX4;
RX PubMed=7744252; DOI=10.1101/gad.9.9.1111;
RA Shaulsky G., Kuspa A., Loomis W.F.;
RT "A multidrug resistance transporter/serine protease gene is required for
RT prestalk specialization in Dictyostelium.";
RL Genes Dev. 9:1111-1122(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Intercellular communication via tagB may mediate integration
CC of cellular differentiation with morphogenesis.
CC {ECO:0000269|PubMed:7744252}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- DISRUPTION PHENOTYPE: Null mutations in either tagB or tagC lead to a
CC cell autonomous defect in prestalk differentiation and a 5-fold
CC reduction in the expression of the prestalk gene ecmA. Disruption of
CC regA in a tagB null or in a tagC null background results in higher
CC levels of sporulation. {ECO:0000269|PubMed:7744252}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ABC transporter
CC superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201)
CC subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peptidase S8
CC family. {ECO:0000305}.
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DR EMBL; U20432; AAA62212.1; -; Genomic_DNA.
DR EMBL; AAFI02000085; EAL64352.1; -; Genomic_DNA.
DR PIR; T18267; T18267.
DR RefSeq; XP_637865.1; XM_632773.1.
DR AlphaFoldDB; P54683; -.
DR SMR; P54683; -.
DR STRING; 44689.P54683; -.
DR MEROPS; S08.A57; -.
DR GlyCosmos; P54683; 8 sites, No reported glycans.
DR PaxDb; 44689-DDB0191217; -.
DR EnsemblProtists; EAL64352; EAL64352; DDB_G0286119.
DR GeneID; 8625462; -.
DR KEGG; ddi:DDB_G0286119; -.
DR dictyBase; DDB_G0286119; tagB.
DR eggNOG; KOG0055; Eukaryota.
DR eggNOG; KOG0058; Eukaryota.
DR HOGENOM; CLU_235711_0_0_1; -.
DR InParanoid; P54683; -.
DR OMA; WISWIGE; -.
DR PhylomeDB; P54683; -.
DR Reactome; R-DDI-159418; Recycling of bile acids and salts.
DR Reactome; R-DDI-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-DDI-382556; ABC-family proteins mediated transport.
DR Reactome; R-DDI-9754706; Atorvastatin ADME.
DR Reactome; R-DDI-9757110; Prednisone ADME.
DR Reactome; R-DDI-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:P54683; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005886; C:plasma membrane; TAS:dictyBase.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IGI:dictyBase.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IMP:dictyBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18557; ABC_6TM_TAP_ABCB8_10_like; 1.
DR CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF625; SERINE PROTEASE_ABC TRANSPORTER B FAMILY PROTEIN TAGB; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Hydrolase; Membrane; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1906
FT /note="Serine protease/ABC transporter B family protein
FT tagB"
FT /id="PRO_0000027191"
FT TRANSMEM 1011..1031
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1076..1096
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1121..1141
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1210..1230
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1309..1329
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1332..1352
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 356..763
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 1080..1363
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1518..1756
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 96..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1757..1906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1760..1786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1816..1867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1868..1884
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 432
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 695
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 1553..1560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1829
FT /note="Missing (in Ref. 1; AAA62212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1906 AA; 212647 MW; CCAAD3D6857CED20 CRC64;
MKFQFSSPSK IFLFSSVILI LIFIGIKFEL LEDTNSNRND KFNNIINRFI NYNIDDSIYK
NKQQQQQFSN KIYSNEKKIL LKNKIIDTTI KPSININNNN NNNNKLNNNN NNNNNNNNNN
NNNNNNNNNN NNNNYYNSIE YYSSFVSRLL KSNDDDGIYY DDYQSKYKKN HYIVQFKDRI
NDETREQLKE FLIGTDITIL KEQPFKSHIV HYIPHDSFLV FMTKEQSVLL SSKEWISWIG
EHEPSNKIHL NYHEKSIGYP VYIILSGSTN SLIQRWENTL NSILTSYNSK VKLTLINQKK
LKSIVYCNDE SPSSSSSSSC SLIGSEKIVY KWISEQSESN YIERSEKLQT ANRLSPTVIF
GTKDKLVNND RIDIPLRGKG QILSIADTGL DGSHCFFSDS KYPIPFNQVN ENHRKVVTYI
TYHDNEDYVN GHGTHVCGSA AGTPEDSSWA ISSFSGLATD AKIAFYDLSS GSSEPTPPED
YSQMYKPLYD AGARVHGDSW GSVSLQGYYG GYSDDAGGID AFLYEYPEFS ILRAAGNNEL
FASLLAQATA KNAITVGAEQ TAHVNYVSDA LEYYDFSDNA NFQRPCLFDK KYCNYTTAKC
CSEVSNVKGL QLCCPASIKQ NASDSFTTQP QFYNENNMGS FSSKGPTHDG RLKPDIVAPG
EYITSARSNG ENSTDQCGDG SLPNANGLMS ISGTSMATPL ATAATTILRQ YLVDGYFPTG
ESVEENKLLP TGSLLKALMI NNAQLLNGTY FWSASSTNPS NAIFEQINGA NLIQGWGALR
MNNWLYVKSS NPTPPSRWIG IGGLGKNQKA TEWKEDSLSS GLNKSYCFTY KPSSSSSGSG
GGGGTPRIVA TLVWTDPPSY SGAKFNLVNN LDLLLLNSDD DSIITIGNSG GSLQPAGKVA
QPDTLNNVEG IIINPTKAMN YKFTIAGTNV PIGPQKFSFV FHGENGQFDW ADSCPQCVDG
VQFPCLITNG IGIQSCGSDL LWTKCIVQSC NEGYNYNSLK NTCDKFLSYN YIIIIVAGGT
MVLIILLLMW IKYQEYKESK RDSFRRFDDG TGIFVRPKDK DAKVTPPDLY NLVSPFIIEL
TIATACSLVA TAASILQPFY IGNIVNNIPT TKSIGEFKSD FIIIFILAFI EFLFTNVGSW
ISGIVNEKMV MRLQNKVFRA LIAQDMGFFQ RNNSALLMNV LIVDTPMLRS ALTGILLSIA
TGVCKLVGSL VFIFTISWKL SLAFFAAVPI LGLVTQIQSQ FTKRLTRQLL FHNSKASQHG
TESLTNMHVV TNYCKQEKEM VKYSDQLMNV FITARKLIIT NTFAGTGKWL LIESLTFVIL
YFSAYLVIQK QFTVGLMISF SLYIGYVVDA SSSLFGVYVS YIQCLASATR VFMILRSAPR
KRTTLEEEEA DRLAGLSGGG GGGGDNGDDK KDKQNIENGK DVLPSNIITP IDNVENSNGK
QDDPNNNNNN IGNLDYSEQL DGVSTVADST VGLTKRELKK QKEKEQKEYF KQTGISVAET
PTFLPSSYTE LTECRGEIEF KNVSFRYPTR PDVQVLHNIN MKFEAGKCYG LVGPSGSGKS
TTLELISKFY PLHGETGGKI YMDGIDIAKI RPNNLRSFVT NVHQHPFLFD ATIGENIGYA
IDNPTQEDII EAAKLAYAHE FINDLPKKYD TQIGEAGNLS GGQKKRIAVA RAICAKRKIM
LLDEITAELD PESEEAITQS IKVLTQGHTV VMVAHKVAAV RDCDKIFVLE KGYLVEEGTH
DELMANKGKY YRMFSEDKDD TPLQNNNNNK NNNNNNNNNE PSSSSTPPND QPTPPPQEQQ
EQKNDQPPPP PPQEQQEQQE QQQQQQQEQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QNDQPPNDYD QVPPPPPLPS ESPSPPTGNN DGQPLVQMDE ENDEER
//
