ID U2ZTX4_PSEA4 Unreviewed; 718 AA.
AC U2ZTX4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative type I secretion system ATP-binding protein {ECO:0000313|EMBL:GAD64890.1};
GN ORFNames=PA6_052_00140 {ECO:0000313|EMBL:GAD64890.1};
OS Pseudomonas alcaligenes (strain ATCC 14909 / DSM 50342 / JCM 20561 / NBRC
OS 14159 / NCIMB 9945 / NCTC 10367 / 1577).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1215092 {ECO:0000313|EMBL:GAD64890.1, ECO:0000313|Proteomes:UP000016560};
RN [1] {ECO:0000313|EMBL:GAD64890.1, ECO:0000313|Proteomes:UP000016560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14909 / DSM 50342 / JCM 20561 / NBRC 14159 / NCIMB 9945 /
RC NCTC 10367 / 1577 {ECO:0000313|Proteomes:UP000016560};
RA Yoshida I., Hosoyama A., Tsuchikane K., Noguchi M., Hirakata S., Ando Y.,
RA Ohji S., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Pseudomonas alcaligenes NBRC 14159.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Protein-1
CC exporter (TC 3.A.1.109) family. {ECO:0000256|ARBA:ARBA00006025}.
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:GAD64890.1}.
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DR EMBL; BATI01000052; GAD64890.1; -; Genomic_DNA.
DR AlphaFoldDB; U2ZTX4; -.
DR eggNOG; COG2274; Bacteria.
DR Proteomes; UP000016560; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd18588; ABC_6TM_CyaB_HlyB_like; 1.
DR CDD; cd02417; Peptidase_C39_likeA; 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; IPR010132; ATPase_T1SS_HlyB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039395; Peptidase_C39-like_A.
DR InterPro; IPR039421; Type_1_exporter.
DR NCBIfam; TIGR01846; type_I_sec_HlyB; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:GAD64890.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016560};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 163..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 274..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..135
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 167..446
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 479..714
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 718 AA; 79127 MW; A680FA6C5FD40DE9 CRC64;
MQGLQMQDEA QGAGASPEPD TGLACLVMLA RFHNVAASPE QLAHEFAEDG RRFGRAELLL
SAKKLGLKAK SARSSLSRLD TTPLPAIAAD HEGRYFIIAR LDDGKALIHD PRAQRPEVLT
FEQLEQRWSG ELLLIRSEAS LAGELSKFDF TWFIPAIVKY RKLLGEVLLV SFVLQIFALL
TPLFFQVVMD KVLVHRGLST LDVIAIGLLG IMVFETLLSG LRSYVFAHTA SRIDVELGSR
LFRHLVTLPL AYFQARRVGD SVARVRELEN IRSFLTGNAI TLILDVLFSV VFIAVMFYYS
GWLTLVVVLS LPLYFLISLL ITPVLRARLN ESFSRGAENQ AFLVETVNGI DTLKAMAVEP
QINRKWDNQL AGYVAASFKT QNLSTIANES VGFVGKLVTV ATLWLGARLV IEGDLTVGQL
IAFNMLAGRV SQPIMRLAQL WTNFQQTGVS VQRLGDILNA RTELSQATRS ALPPLKGQIE
FDQVHFRYRP DGSEVLRGVS LQIHAGEVIG VVGRSGSGKS TLTRLLQRLY TPERGRVLVD
GMDLALADVS SLRRQIGVVL QDNMLFARSI RENIALTDPG APLEAVIQAA KLAGAHEFIL
ELPEGYDTVV GEHGASLSGG QRQRIAIARA LIGNPRVLIF DEATSALDYE SERVIQQNMQ
AICKGRTVII IAHRLSAVRD ANRIVVMDRG QIVEQGSHAE LLSHQAGHYS RLHRLQQG
//
