ID A0A090AJY5_9GAMM Unreviewed; 725 AA.
AC A0A090AJY5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=ABC transporter {ECO:0000313|EMBL:BAP55902.1};
GN ORFNames=THII_1605 {ECO:0000313|EMBL:BAP55902.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP55902.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP55902.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AP014633; BAP55902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090AJY5; -.
DR STRING; 40754.THII_1605; -.
DR KEGG; tig:THII_1605; -.
DR HOGENOM; CLU_000604_95_6_6; -.
DR OrthoDB; 9806127at2; -.
DR Proteomes; UP000031623; Chromosome.
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 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; 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:UP000031623};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..141
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 177..455
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 489..724
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 725 AA; 80421 MW; E6B8A3AFC74A6F14 CRC64;
MTTNHFDSNA WQESERIIIF DDPLLQCLVI LTKLLSKPVS AEALKAGLPL VNNRFTPELF
IRAAERAHLS AQLLKRSLAQ FNPLMLPAVL LLKDQQACIL VKYLDKKKKQ AQIILPMTGE
GTLTISRKDL QANYSGYALL ARPTYTFDQR TAQDIIPHSR SWFWGTLLKS WSIYSEVIIA
SLLINLFALA SPLFVMNVYD RVVPNRAIET LWVLAIGVGI VFSFDFIMRI LRGYFIDIAG
KKSDVLLASI IFEQILGTQR AAHPRSIGAF ANHLHEFETF RDFFTSATLT TLVDLPFALL
FIAVIWTLNP ELAMIPLYSM AIVMGLSLLL QLPLRYVVRQ TFRASAQKHA LLIETLSGIE
TLKARGAEGE MQRKWELLIG QIAQSSLKSR FLSALAVNFS LFVQQITTIV VVVTGVYLIA
DGKLTTGALI ASTILTGRAL APLAPIANLL TRYHQSLSAL RVLNHIMSMP LERPLGKPFL
HRPQLRGDIE FKQVDFNYPQ QPVAALTKMS FKISAGQRVG IIGRIGSGKS TLAKLILGLY
QPTGGSILLD GVDSRQLDPA ELRRNIGYVP QDLELFYGTV KDNIVIGASY VEDSMVLKAA
QLAGVDEFIN RHPLGFDMLI GERGEGLSGG QRQTIVLARA LLLNPPILLL DEPTNAMDNR
AEELLKARLQ PYLEDKTLLL VTHRMSLLSL VNHLIVVDGG QIVAFGLKEQ VIQALTSGQV
KMSNN
//
