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Database: UniProt
Entry: A0A0Q7YXG3_9SPHN
LinkDB: A0A0Q7YXG3_9SPHN
Original site: A0A0Q7YXG3_9SPHN 
ID   A0A0Q7YXG3_9SPHN        Unreviewed;       712 AA.
AC   A0A0Q7YXG3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=NHLP family bacteriocin export ABC transporter peptidase/permease/ATPase subunit {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASD67_13620 {ECO:0000313|EMBL:KQZ62561.1};
OS   Sphingopyxis sp. Root1497.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ62561.1, ECO:0000313|Proteomes:UP000051141};
RN   [1] {ECO:0000313|Proteomes:UP000051141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1497 {ECO:0000313|Proteomes:UP000051141};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ62561.1, ECO:0000313|Proteomes:UP000051141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1497 {ECO:0000313|EMBL:KQZ62561.1,
RC   ECO:0000313|Proteomes:UP000051141};
RA   Schulze-Lefert P.;
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:KQZ62561.1}.
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DR   EMBL; LMGF01000004; KQZ62561.1; -; Genomic_DNA.
DR   RefSeq; WP_056348042.1; NZ_LMGF01000004.1.
DR   AlphaFoldDB; A0A0Q7YXG3; -.
DR   STRING; 1736474.ASD67_13620; -.
DR   OrthoDB; 9787557at2; -.
DR   Proteomes; UP000051141; Unassembled WGS sequence.
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; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR022514; NHPM_micro_ABC1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_1_exporter.
DR   NCBIfam; TIGR03796; NHLM_micro_ABC1; 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        160..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        389..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        420..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..131
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          162..443
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          479..712
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   712 AA;  76707 MW;  E87B81CCB66CF550 CRC64;
     MARRRSTPTV LQLEAAECGA ASLAMVLAAH GRHMGLDELR ALCGVSRDGT KASSLLRAAR
     ALGLEAKGLK AEPEHIADLP LPAIAFVHFN HFLVVEHIDA RHVWLNDPAS GRRRETIAEF
     SDGFTGVVLT FVPGAGFERG DSRPSLAQSL RQRFDGVRTA LWFVVLTALA LVVPGVVLPV
     FSRIFVDYVL VRGLSDWLLP LLIGMALTAL VRFILLELQE RTLLRARMAM SLNTGGALMR
     KLLTLPVAFF DQRFAGEIAD RVKLNESLAT LLTGHLAQAA VNLVSALFFL IVLLFYHWAL
     TLAIAALALL NAAVLLLSNR LLSDRYRKIS IDRGKLAGAR VAGLKDMETF KASGGEDMLF
     ARWTGLTIAV QNGEQQVARL AAFVQPMPAL ISALIIATIL VWGGFAVMGG TMTLGELVGY
     QTLAASFVAP VAALAGFGAE LHQIRSYTGR LDDVLAEASD PRFDRADPAS DGRLPQGGVS
     ARDLSFGYAP LDPPLIDGLS FDLLPGERIA LVGPSGSGKS TVGKLIAGLE QPRGGDLLLD
     DRALLDWPRA ALAHRLAYVR QDVMLFEGSV RDNLTLWNDA LPEPDMIRAA RDAMIHDVIA
     ARPGGYDARI AQGGGNFSGG ERQRIEIARA LASDPSLIIL DEATSALDPV TEHGVMEAIR
     RRGITCIIIA HRLSAIRDCD RIFVLEQGRV VEAGDHGELM AGRGVYARLV EA
//
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