APRD_PSEAE
ID APRD_PSEAE Reviewed; 593 AA.
AC Q03024;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Alkaline protease secretion ATP-binding protein AprD;
GN Name=aprD; OrderedLocusNames=PA1246;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1427098; DOI=10.1016/0378-1119(92)90160-q;
RA Duong F., Lazdunski A., Cami B., Murgier M.;
RT "Sequence of a cluster of genes controlling synthesis and secretion of
RT alkaline protease in Pseudomonas aeruginosa: relationships to other
RT secretory pathways.";
RL Gene 121:47-54(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Involved in the secretion of alkaline protease.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Alkaline
CC protease exporter (TC 3.A.1.110.4) family. {ECO:0000305}.
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DR EMBL; X64558; CAA45855.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04635.1; -; Genomic_DNA.
DR PIR; S26696; S26696.
DR RefSeq; NP_249937.1; NC_002516.2.
DR RefSeq; WP_003082539.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q03024; -.
DR SMR; Q03024; -.
DR STRING; 287.DR97_691; -.
DR TCDB; 3.A.1.110.4; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q03024; -.
DR PRIDE; Q03024; -.
DR EnsemblBacteria; AAG04635; AAG04635; PA1246.
DR GeneID; 881263; -.
DR KEGG; pae:PA1246; -.
DR PATRIC; fig|208964.12.peg.1293; -.
DR PseudoCAP; PA1246; -.
DR HOGENOM; CLU_000604_95_6_6; -.
DR InParanoid; Q03024; -.
DR OMA; SIMMGRA; -.
DR PhylomeDB; Q03024; -.
DR BioCyc; PAER208964:G1FZ6-1271-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR GO; GO:0046903; P:secretion; IDA:PseudoCAP.
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; IPR010128; ATPase_T1SS_PrtD-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24222:SF0; PTHR24222:SF0; 1.
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 TIGRFAMs; TIGR01842; type_I_sec_PrtD; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..593
FT /note="Alkaline protease secretion ATP-binding protein
FT AprD"
FT /id="PRO_0000091933"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 248..266
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 23..301
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 332..567
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 366..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 593 AA; 63671 MW; CA3A817FBCC27318 CRC64;
MARLGSSVTN EIKQALAASR GALRSVAAFS GVINLLMLVP SLYMLQVYDR VLSSANEVTL
LMLTLMALGV FVFMGALEAL RSFVLVRVSE RFDGQLHGRI YAAAFERNLR AGGQEASQAL
HDLTTLRQFI TGQALFAFFD APWFPVYLLV IFLFDPWLGL LSLVGALALM ALAWFNERAT
RAPLAKAGEL SIKSGQLASN NLRNAEVIEA MGMLGSMRGR WERLHQAFLD QQSLASERAA
RINALSKYLR IALQSLVLGL GAWLAVEGRI TPGMMIAGSI LMGRALGPID QLIGVWKQWG
AARDAYRRLS GLLDEFPARE RRMELPEPRG HLLLESLDAA PPGSEARTLR GLTLAIPAGS
VVGVIGPSGS GKSSLARVVL GIWPTLHGSV RLDGAEIRQY ERETLGPRIG YLPQDIELFA
GTVAENIARF GEVQADKVVE AARLAGVHEL VLRLPQGYDT VLGVGGAGLS GGQRQRIALA
RALYGAPTLV VLDEPNSNLD DSGEQALLAA IQALKARGCT VLLITHRAGV LGCADRLLAL
NAGQLHLYGE RDQVLAALNN QRAASASQQR ADYRVAGYGA PQVVAAPRQG GVE
