ID Q1DBD6_MYXXD Unreviewed; 909 AA.
AC Q1DBD6;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=ABC transporter, ATP-binding protein/peptidase, C39 family {ECO:0000313|EMBL:ABF86513.1};
GN OrderedLocusNames=MXAN_1789 {ECO:0000313|EMBL:ABF86513.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF86513.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF86513.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000113; ABF86513.1; -; Genomic_DNA.
DR RefSeq; WP_011551896.1; NC_008095.1.
DR AlphaFoldDB; Q1DBD6; -.
DR STRING; 246197.MXAN_1789; -.
DR EnsemblBacteria; ABF86513; ABF86513; MXAN_1789.
DR GeneID; 41359210; -.
DR KEGG; mxa:MXAN_1789; -.
DR eggNOG; COG1132; Bacteria.
DR eggNOG; COG3271; Bacteria.
DR HOGENOM; CLU_322031_0_0_7; -.
DR OrthoDB; 5495812at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0016020; C: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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ABF86513.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 304..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 555..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..142
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 309..587
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 625..859
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 889..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 99027 MW; D8CFA1B112BDDDC9 CRC64;
MTPPRRRRSI IPEVIQISAT DCGPASLKSL FAGMGAELNY RVLREVCQTD VDGTSIVTLD
EVANQLGLDA EQVMLPLDHV VVPEAKALPA IIVTLSAGGR PHFVVLWNRV GPFIQVMDPA
AGRHWTRIST LLSHLYQHTT SVPATGWREW AGSEEAVATF ERRLLNLGAT QARALVARAL
KDPGYLSIAR LDAACRASEA MIRAGAVRRG RMAAGLLQSM IAKDDSSEVP IPAAYWSVRP
NPEVEGELSM TGAVLMRVRG WREAPREGED APRAVLASDL ATELIAKQVS PARTLLRLRG
EDSWVVPGLI AVGLVFATFG RILQSLMLRG VLDLGRDLGT FAQRATGMAV LAGVALCFML
IQIPISLGLL GIGRRLEVRL RKAYFEKLPE MEDRYFQSRL ASDMASRTHN IQAMRSLPPL
LAQALVLSLE VASITAALIW AAPHAWRIVL ALAAVTLLVP LVAQKLLFEP DLRVQMHAGA
LSGFTLNALV GLTPIRIHGA ERSLRRAQET LLVSWSKARY WLQTLSVGFE GGLMLGSYGL
VMLLVYSYLA GTDRASLVLL VVYWALRFPI LGQRLMMLSR AFPNAMNRVR RLLDVIGDIK
EPPARPEAPV QEPVAPADAA SGVSIVMEKV RVKGGGHTIL DKVSLNIAPG EHVAVVGVSG
AGKSTLVGLL LGWLRPARGE IKVDGQVLDQ AAVERLRRTT AWVDPAISLW NQSLIDNLRY
GNDGAHGWSL SGALKSAEML DILEALPDGL QTSLGEGGGL VSGGQGQRVR LARAMLRSGV
RLAILDEPFR GLDRDRRARL LAESRRLWAD ITLLCVTHDV EHTQEFDRVL VIENGRILEN
GPPKELLANK ESRYAVLLRA DQENRTLLWG GGRWRHWWLS DGQLVERPAP KPVETPVAEP
AAGGLELAG
//
