ID A0A060RAW6_9BACT Unreviewed; 732 AA.
AC A0A060RAW6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:CDN30529.1};
GN ORFNames=BN938_0424 {ECO:0000313|EMBL:CDN30529.1};
OS Mucinivorans hirudinis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Mucinivorans.
OX NCBI_TaxID=1433126 {ECO:0000313|EMBL:CDN30529.1, ECO:0000313|Proteomes:UP000027616};
RN [1] {ECO:0000313|EMBL:CDN30529.1, ECO:0000313|Proteomes:UP000027616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|Proteomes:UP000027616};
RX PubMed=25657285; DOI=10.1128/genomeA.01530-14;
RA Nelson M.C., Bomar L., Graf J.;
RT "Complete Genome Sequence of the Novel Leech Symbiont Mucinivorans
RT hirudinis M3T.";
RL Genome Announc. 3:e01530-e01514(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HG934468; CDN30529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060RAW6; -.
DR STRING; 1433126.BN938_0424; -.
DR KEGG; rbc:BN938_0424; -.
DR PATRIC; fig|1433126.3.peg.421; -.
DR eggNOG; COG2274; Bacteria.
DR HOGENOM; CLU_000604_95_3_10; -.
DR OrthoDB; 9760358at2; -.
DR Proteomes; UP000027616; Chromosome I.
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:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd18571; ABC_6TM_peptidase_like; 1.
DR CDD; cd02418; Peptidase_C39B; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
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; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:CDN30529.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027616};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 173..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..128
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 175..456
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 490..726
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 732 AA; 81582 MW; C16072FBE525908B CRC64;
MKFPHYFQLD SMDCGATCLR MVARFYGKGY PAAFFRERCH TTREGVSMLG ISDAAEGVGF
RTMGVKISFE QLCNEVNLPC IVHWNQNHFA VVYNIKRGKI YIADPAAGLL CYDKERFLKS
WLSTSSEGSE LTLTQGTALL LEPTPRFYEE EAPDESKLHF GHLLRYLTPY KRYIIQLFLG
LLTGSLISLI FPFLTQSVVD TGIGNNDINI VIAILIAQVM LTLGQTANDL IKSWLMLHIT
TRISISLISD FLGKLMRLPI AFFDSKMVGD IMQRIGDHSR IQSFLTGSII SIAVAAITFV
IYSGVMASYN LPILGVFVLG SALYVGWILI FLKRRRKLDY MRFQEAAANQ SNIVQLINGM
QDIKLNNCEK QKRWVWEGIQ AKLYKISIKG LTLQQTQQVG GLFIDQSKNV FISFLAATAV
INGEMTLGMM MAMQYIIGQL NAPLSQFIGF VQESQDAKIS LERLNEIHSK DDEEPASKSK
IREIPTGEDI VLRNVVFQYE GPNSEKVLND VSLTIEAGKV TAIVGTSGSG KTTLLKLLLG
FYEPASGEVL LGSVPLKMYS DTVWRGHCAA VMQEGYIFSD TIAGNIGVMD EVPNMKRVNK
AVDIANIREF IESLPLRYNT KIGSDGHGLS TGQKQRLLIA RAAYKEAEYI MFDEATNSLD
ANNERVIMDK LQGFFRGKTV VVVAHRLSTV RSADKIVVLE GGEVVEQGTH QELVASRGAY
YELVRNQLEL GT
//
