ID   PRTD_DICCH              Reviewed;         575 AA.
AC   P23596;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Proteases secretion ATP-binding protein PrtD;
GN   Name=prtD;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2184029; DOI=10.1002/j.1460-2075.1990.tb08252.x;
RA   Letoffe S., Delepelaire P., Wandersman C.;
RT   "Protease secretion by Erwinia chrysanthemi: the specific secretion
RT   functions are analogous to those of Escherichia coli alpha-haemolysin.";
RL   EMBO J. 9:1375-1382(1990).
CC   -!- FUNCTION: Involved in the secretion of proteases A, B, C and G.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M60395; AAA63634.1; -; Genomic_DNA.
DR   EMBL; X53253; CAA37342.1; -; Genomic_DNA.
DR   PIR; S12525; S12525.
DR   AlphaFoldDB; P23596; -.
DR   SMR; P23596; -.
DR   TCDB; 3.A.1.110.11; the atp-binding cassette (abc) superfamily.
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: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:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
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 inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..575
FT                   /note="Proteases secretion ATP-binding protein PrtD"
FT                   /id="PRO_0000092763"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          22..300
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          331..565
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         364..371
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   575 AA;  61617 MW;  1BCEC4E74B1B92D6 CRC64;
     MNASSERDRS LFGVLRQFRR SFWSVGIFSA VINVLMLAPS VYMLQVYDRV LASGNGITLL
     MLTLLMAGLC AFMGALEWVR SLLVVRLGTR IDLALNQDVF NAAFARNLEA GDGRAGLALT
     DLTLLRQFIT GNALFAFFDV PWFPLFLLVL FLLHPWLGML ALGGTVVPGG VGLAEPASDQ
     STAGGSNQQS QQATHLADAQ LRNADVIEAM GMLGNLRRRW LARHYRFISL QNLASERAAA
     VGGASKYSRI ALQSLMLGLG ALLAIDGKIT PGMMIAGSIL VGRVLSPIDQ LIGVWKQWSS
     ARIAWQRLTR LIAAYPPRPA AMALPAPEGH LSVEQVSLRT AQGNTRLQNI HFSLQAGETL
     VILGASGSGK SSLARLLVGA QSPTQGKVRL DGADLNQVDK NTFGPTIGYL PQDVQLFKGS
     LAENIARFGD ADPEKVVAAA KLAGVHELIL SLPNGYDTEL GDGGGGLSGG QRQRIGLARA
     MYGDPCLLIL DEPNASLDSE GDQALMQAIV ALQKRGATVV LITHRPALTT LAQKILILHE
     GQQQRMGLAR DVLTELQQRS AANQARMNPT AAMPQ