ID A7I394_CAMHC Unreviewed; 699 AA. AC A7I394; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 99. DE SubName: Full=Leukotoxin translocation ATP-binding protein LktB {ECO:0000313|EMBL:ABS50954.1}; DE EC=3.6.3.43 {ECO:0000313|EMBL:ABS50954.1}; GN OrderedLocusNames=CHAB381_1446 {ECO:0000313|EMBL:ABS50954.1}; OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / OS CH001A). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360107 {ECO:0000313|EMBL:ABS50954.1, ECO:0000313|Proteomes:UP000002407}; RN [1] {ECO:0000313|Proteomes:UP000002407} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A RC {ECO:0000313|Proteomes:UP000002407}; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., Nelson K.E.; RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a RT commensal isolated from the human gastrointestinal tract."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000776; ABS50954.1; -; Genomic_DNA. DR RefSeq; WP_012109288.1; NC_009714.1. DR AlphaFoldDB; A7I394; -. DR STRING; 360107.CHAB381_1446; -. DR KEGG; cha:CHAB381_1446; -. DR eggNOG; COG2274; Bacteria. DR HOGENOM; CLU_000604_95_4_7; -. DR OrthoDB; 9760168at2; -. DR Proteomes; UP000002407; Chromosome. 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 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; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ABS50954.1}; KW Hydrolase {ECO:0000313|EMBL:ABS50954.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000002407}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 140..162 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 174..196 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 258..277 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 283..303 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 2..115 FT /note="Peptidase C39" FT /evidence="ECO:0000259|PROSITE:PS50990" FT DOMAIN 145..424 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000259|PROSITE:PS50929" FT DOMAIN 457..692 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" SQ SEQUENCE 699 AA; 78584 MW; 4A3B89AD9E77F57F CRC64; MRTALQALAL ITQINRIPFD SKEIINKFAL NTNEPSIDEL TRIAKYLEFK AKIKNISEIS KYKPPFIAQS KQNTYFVIFQ ILEDGSFLIY DGGSSLKKIN KDEMNEISNS KIIVLAHKAL NSQVKFGFAW FYKKMLKFKF IIFEVLLASF IMQLFGLVTP LFTQVVLDKV LTHHSISTLN VIAVAFFAVI IFEMLLSLTR NYIFAHTTTK IDAQLGSELF LHLLLLPMTY FENRKVGNIA ARVRELDSIR DFIANKSVTV LLDLLFSFVF VIMMLLYSVK LTLIAIAFVS VIALIYFFIT PMLRARLNDK FEMGARSNSY LIESITGMQT VKSLAIEGGM QRNWEDYLAK YVKSSFNLSN LSNIASGFAN ALSKLMTLSI LYFGVGLVIE GKLSVGQLIA FQMFAGQFAS PVMRLVGLWN EFQQAIISVD KLGDILNTPT EQTTNKPISL NKVRGEIKFE NVSFRYNPGS NLVLKNLSFK IDANKSVGIV GKSGSGKSTI TKLIERLYLQ NDGAIYIDDI DIRHLNPYIL RQNIGVVLQE NYLFSGTIRE NISYAKADAS MDEIIKVAKI SGAHDFIKEL SSGYDTIVGE RGSSLSGGQK QRIAIARAII SNPKILIFDE ATSALDYESE KAITENLNKI KENRTFIIIA HRLSTIRNCD EIIVIDKGEI KERGSHDELV AKNGYYKKLL DAQAGLNHV //