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Database: UniProt
Entry: D0I8X2_GRIHO
LinkDB: D0I8X2_GRIHO
Original site: D0I8X2_GRIHO 
ID   D0I8X2_GRIHO            Unreviewed;       705 AA.
AC   D0I8X2;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=ABC transporter transmembrane region {ECO:0000313|EMBL:EEY71887.1};
GN   ORFNames=VHA_002309 {ECO:0000313|EMBL:EEY71887.1};
OS   Grimontia hollisae CIP 101886.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY71887.1, ECO:0000313|Proteomes:UP000003604};
RN   [1] {ECO:0000313|EMBL:EEY71887.1, ECO:0000313|Proteomes:UP000003604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY71887.1,
RC   ECO:0000313|Proteomes:UP000003604};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA   Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA   Bartels D., Vonstein V.;
RL   Submitted (OCT-2009) 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:EEY71887.1}.
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DR   EMBL; ADAQ01000012; EEY71887.1; -; Genomic_DNA.
DR   RefSeq; WP_005504637.1; NZ_ADAQ01000012.1.
DR   AlphaFoldDB; D0I8X2; -.
DR   GeneID; 58894279; -.
DR   eggNOG; COG2274; Bacteria.
DR   OrthoDB; 9782586at2; -.
DR   Proteomes; UP000003604; 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:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd18587; ABC_6TM_LapB_like; 1.
DR   CDD; cd03245; ABCC_bacteriocin_exporters; 1.
DR   CDD; cd02421; Peptidase_C39_likeD; 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; IPR017750; ATPase_T1SS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_1_exporter.
DR   NCBIfam; TIGR03375; type_I_sec_LssB; 1.
DR   PANTHER; PTHR24221:SF248; ABC TRANSPORTER TRANSMEMBRANE REGION-RELATED; 1.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000003604};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        158..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..122
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          158..436
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          470..705
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   705 AA;  78553 MW;  F3BAC12860A8E7A9 CRC64;
     MVKDPLLQSL VYVSRYFGQS NSPDALISGL PISDGYLSPF LFRRAAERAG IDAKESRQTL
     GSLSPMLCPC ILLLKDNQAC VLLSIDHETG EAEVVEPLTD TSPVARKIDD LEDDYLGRVF
     LLKKQFRYDE RSPEILKERQ GHWFWSTLWE SRSIYRDVLI ASIFINAFAI ATPLFSRIVY
     DKIVPNLAFD SLWVLATGVF VIFLFDLVLK MLRSYFIDIS GKKSDLLISS RIFEKVMGIR
     MEARPPSVGA FARHMQEFES IRDFFTSASV STLIDLPFAF FFLLIIWIVA GPLVIVPIMA
     VLLLMLHAAL IQKPLRHTIE EGSRLSSQKN ANLIESLTGL ETIKLFGAES QFQYRWEEAV
     AHMANWGIKT RRLTDSVQNA AGFIQQFVNV SMIVFGVYLI SAGDLSMGGL IAATMLSSRA
     VGPMVQLSLL STRYNQAKSA MTIISQLMDM PSEQEEGKRY IHRPIIRGKI EFDRVNFHYP
     NSDIAALRDI SFTILPGEKV AIIGRIGSGK TTLSRLLMGL YHPTAGSVRI DDTDISQIHN
     IDIRRSIGCV PQDPVLFFGS IRDNITLGRP LADDRDILDA ANRSGVTTFT QRDPAGLERQ
     VGEGGNQLSG GQRQSIAIAR AMLGRPPVLL LDEPTSAMDN RSEQYIKQQL SSLRRDETLI
     INTHKTGMLD VVDRIIVVEQ GNIVADGPKL AVLQALKDGK VQKVG
//
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