ID I1DWX4_9GAMM Unreviewed; 738 AA.
AC I1DWX4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=ATP-binding cassette, subfamily B, bacterial HlyB/CyaB {ECO:0000313|EMBL:GAB58552.1};
GN ORFNames=RNAN_1525 {ECO:0000313|EMBL:GAB58552.1};
OS Rheinheimera nanhaiensis E407-8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB58552.1, ECO:0000313|Proteomes:UP000004374};
RN [1] {ECO:0000313|EMBL:GAB58552.1, ECO:0000313|Proteomes:UP000004374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E407-8 {ECO:0000313|EMBL:GAB58552.1,
RC ECO:0000313|Proteomes:UP000004374};
RX PubMed=23209246; DOI=10.1128/JB.01922-12;
RA Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., Zhou B.-C.,
RA Zhang Y.-Z.;
RT "Genome Sequence of the Protease-Producing Bacterium Rheinheimera
RT nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South China
RT Sea.";
RL J. Bacteriol. 194:7001-7002(2012).
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:GAB58552.1}.
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DR EMBL; BAFK01000007; GAB58552.1; -; Genomic_DNA.
DR RefSeq; WP_008220329.1; NZ_BAFK01000007.1.
DR AlphaFoldDB; I1DWX4; -.
DR STRING; 562729.RNAN_1525; -.
DR OrthoDB; 9759820at2; -.
DR Proteomes; UP000004374; 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 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:GAB58552.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000004374};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 151..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..123
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 155..434
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 468..703
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 738 AA; 81096 MW; 1E56A339DC7FF7DF CRC64;
MSQNSPFAVG VQCLAIVARM QQTPAEVSSL LREFTPQSDD LNDIYLVKAA KSLGFKAKFI
AVAPDKLDAL LLPAVGKTQD GGYFILARIK DNNALIQNVT TGQVQSVPLI NLAKMWTGEL
LHLTKRASLL DDKTRFGFRW FIPALIKYRH LFADVLMASF FIQLVGLATP IFFQVTIDKV
LVHKGMTTLD VLAVGFFAVI TFEVLLTALR TYVFSHTTNR VDVELGGQLY RHMLSLPISY
FAARRVGDTV ARIKELDKVR EFITGSSLTV VLDVLFSVVF FAVMFYYAPL LSWIIVGSIP
CYILLSVLIT PTLRAKLEQK FQKSAENHSF LVESVSGVET VKSLAVEPQM RNKWEEKLAD
YVASSFDASH INNIYASIAN YINKVVSLLT LYFGAIAVVE GSLTVGQFIA FNMLSQRVSG
PIMRLVNLWQ DFQQAKVSIE RLGDVLNAPT EPGYNPNRTA LPAVQGQVSL QQVSFRYRPD
SAPILNNVSM DIAAGERIGI VGRSGSGKST LTKLIQRLYV PQGGRVLIDG IDLALVEPAW
LRRQVGVVLQ ESFLFNRSIR DNIALSDPGS SIEQVIQAAK LAGAHEFICE LSEGYDTVVG
EHGASLSGGQ RQRLAIARAL IANPKILIFD EATSALDYES ERIIQTNMAQ ICAGRTVFII
AHRLSAVRDC NRIIVMDKGQ IAEQGSHTEL LKQQGIYHYL MQIQHGGPAA AANPNHTSAA
VQVASLLPQA VAGKGERP
//
