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Database: UniProt
Entry: A0A0Q4GTE2_9SPHI
LinkDB: A0A0Q4GTE2_9SPHI
Original site: A0A0Q4GTE2_9SPHI 
ID   A0A0Q4GTE2_9SPHI        Unreviewed;       752 AA.
AC   A0A0Q4GTE2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Peptidase C39 {ECO:0000313|EMBL:KQM76267.1};
GN   ORFNames=ASE74_19635 {ECO:0000313|EMBL:KQM76267.1};
OS   Pedobacter sp. Leaf216.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1735684 {ECO:0000313|EMBL:KQM76267.1, ECO:0000313|Proteomes:UP000051744};
RN   [1] {ECO:0000313|Proteomes:UP000051744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA   Garrido-Oter R., Mueller D.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQM76267.1}.
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DR   EMBL; LMKM01000009; KQM76267.1; -; Genomic_DNA.
DR   RefSeq; WP_055907043.1; NZ_LMKM01000009.1.
DR   AlphaFoldDB; A0A0Q4GTE2; -.
DR   STRING; 1735684.ASE74_19635; -.
DR   OrthoDB; 9760358at2; -.
DR   Proteomes; UP000051744; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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: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   CDD; cd18570; ABC_6TM_PCAT1_LagD_like; 1.
DR   CDD; cd02418; Peptidase_C39B; 1.
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; 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   NCBIfam; TIGR01193; bacteriocin_ABC; 1.
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; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        180..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        217..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        410..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..151
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          184..463
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          496..731
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   752 AA;  84424 MW;  3478531671D91072 CRC64;
     MKSLSQIFKA FSSKLASNKK AKRTLIKQHD VTDCGAACLA SISIHYGLDL PIARIRQYAG
     TDKKGTNVLG LIEASSRLGF SAKGVKASYD NLFTIPTPVI AHVNHNNLAH YVVLYKVTEN
     YVEVMDPAYG EMQRLTPNEF KQKWTGVLIM LLPGDDFTAG TERISLEKRF LYLLMPHKSI
     LVQVLIGAIF YTILGLSTSI FLQKIVDNVL PEGNTNLLNL MGTVMIIIIL LQIFINYAKT
     LLTIKTGQQI DARLILGYYK HLLKLPQAFF DTMRVGEIIS RMNDAVKIRA FINDVLVGFA
     VNIFILIFSF ALMFTYYWKL ALIMLTVVPL YALVYYISNR LNKTTQRQLM EKSAELENQL
     VESVNSVSTI KRFGLENFSN LKTEIRFINL LKTVYTSGTN SLLVGNASGF ISSTFSVILL
     WAGASFVLQN LITPGELLSF YAIIGYFTGP VISLIGMNKV FQDARIAADR LFEIMDLERE
     KTENRMDITT DMIGDIEFKK VNFRYGTRVT VFEGFDLYIP KGKITAVVGE SGSGKTTLLS
     LLQNIYPLQS GSIMIGEFDL NYITNESLRK LVAVVPQDVH LFAGNVIENI AVGEMEPDMK
     KIIRICAQLN IMDFIERLPN GFDTYLGENA TNLSGGQRQR LAIARALYRD PEILILDEAT
     SSLDSSSEEH IHNAISLLRE QGKTIILIAH RLSTVVNADK IVVLKEGKLI EEGTHQELVK
     LDGMYTSMWH KQFPSINDAI KRTKTRKVEP KN
//
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