PEDD_PEDAC
ID PEDD_PEDAC Reviewed; 724 AA.
AC P36497;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Pediocin PA-1 transport/processing ATP-binding protein PedD;
DE EC=3.4.22.-;
DE EC=7.-.-.-;
DE AltName: Full=Pediocin AcH transport ATP-binding protein PapD;
GN Name=pedD; Synonyms=papD;
OS Pediococcus acidilactici.
OG Plasmid pSRQ11, and Plasmid pSMB74.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=1254;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAC-1.0; PLASMID=pSRQ11;
RX PubMed=1514784; DOI=10.1128/aem.58.8.2360-2367.1992;
RA Marugg J.D., Gonzalez C.F., Kunka B.S., Ledeboer A.M., Pucci M.J.,
RA Toonen M.Y., Walker S.A., Zoetmulder L.C.M., Vandenbergh P.A.;
RT "Cloning, expression, and nucleotide sequence of genes involved in
RT production of pediocin PA-1, and bacteriocin from Pediococcus acidilactici
RT PAC1.0.";
RL Appl. Environ. Microbiol. 58:2360-2367(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H; PLASMID=pSMB74;
RX PubMed=7764941; DOI=10.1111/j.1472-765x.1994.tb00876.x;
RA Motlagh A.M., Bukhtiyarova M.B., Ray B.R.;
RT "Complete nucleotide sequence of pSMB 74, a plasmid encoding the production
RT of pediocin AcH in Pediococcus acidilactici.";
RL Lett. Appl. Microbiol. 18:305-312(1994).
CC -!- FUNCTION: Involved in the export process of the bacteriocin pediocin
CC PA-1/AcH. Is also essential for pediocin production.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Pediocin PA-1
CC exporter (TC 3.A.1.112.2) family. {ECO:0000305}.
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DR EMBL; M83924; AAA25561.1; -; Genomic_DNA.
DR EMBL; U02482; AAC43296.1; -; Genomic_DNA.
DR PIR; D48941; D48941.
DR RefSeq; NP_857605.1; NC_004832.1.
DR RefSeq; WP_002834569.1; NZ_SCHZ01000012.1.
DR AlphaFoldDB; P36497; -.
DR SMR; P36497; -.
DR MEROPS; C39.001; -.
DR TCDB; 3.A.1.112.2; 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:0043214; F:ABC-type bacteriocin transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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 InterPro; IPR005897; Pept_C39_ABC_bacteriocin.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 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; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR01193; bacteriocin_ABC; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 3: Inferred from homology;
KW ATP-binding; Bacteriocin transport; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Plasmid; Protease; Protein transport; Thiol protease;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..724
FT /note="Pediocin PA-1 transport/processing ATP-binding
FT protein PedD"
FT /id="PRO_0000092682"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 13..140
FT /note="Peptidase C39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT DOMAIN 170..452
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 486..722
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT ACT_SITE 19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT BINDING 519..526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 724 AA; 81652 MW; B897C680EB519AF5 CRC64;
MWTQKWHKYY TAQVDENDCG LAALNMILKY YGSDYMLAHL RQLAKTTADG TTVLGLVKAA
KHLNLNAEAV RADMDALTAS QLPLPVIVHV FKKNKLPHYY VVYQVTENDL IIGDPDPTVK
TTKISKSQFA KEWTQIAIII APTVKYKPIK ESRHTLIDLV PLLIKQKRLI GLIITAAAIT
TLISIAGAYF FQLIIDTYLP HLMTNRLSLV AIGLIVAYAF QAIINYIQSF FTIVLGQRLM
IDIVLKYVHH LFDLPMNFFT TRHVGEMTSR FSDASKIIDA LGSTTLTLFL DMWILLAVGL
FLAYQNINLF LCSLVVVPIY ISIVWLFKKT FNRLNQDTME SNAVLNSAII ESLSGIETIK
SLTGEATTKK KIDTLFSDLL HKNLAYQKAD QGQQAIKAAT KLILTIVILW WGTFFVMRHQ
LSLGQLLTYN ALLAYFLTPL ENIINLQPKL QAARVANNRL NEVYLVESEF SKSREITALE
QLNGDIEVNH VSFNYGYCSN ILEDVSLTIP HHQKITIVGM SGSGKTTLAK LLVGFFEPQE
QHGEIQINHH NISDISRTIL RQYINYVPQE PFIFSGSVLE NLLLGSRPGV TQQMIDQACS
FAEIKTDIEN LPQGYHTRLS ESGFNLSGGQ KQRLSIARAL LSPAQCFIFD ESTSNLDTIT
EHKIVSKLLF MKDKTIIFVA HRLNIASQTD KVVVLDHGKI VEQGSHRQLL NYNGYYARLI
HNQE
