ID Q31VE2_SHIBS Unreviewed; 894 AA.
AC Q31VE2;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=ATP-binding component of a transport system, 1 {ECO:0000313|EMBL:ABB67966.1};
GN Name=yhiH {ECO:0000313|EMBL:ABB67966.1};
GN OrderedLocusNames=SBO_3481 {ECO:0000313|EMBL:ABB67966.1};
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268 {ECO:0000313|EMBL:ABB67966.1, ECO:0000313|Proteomes:UP000007067};
RN [1] {ECO:0000313|EMBL:ABB67966.1, ECO:0000313|Proteomes:UP000007067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227 {ECO:0000313|EMBL:ABB67966.1,
RC ECO:0000313|Proteomes:UP000007067};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000036; ABB67966.1; -; Genomic_DNA.
DR AlphaFoldDB; Q31VE2; -.
DR KEGG; sbo:SBO_3481; -.
DR HOGENOM; CLU_000604_16_3_6; -.
DR Proteomes; UP000007067; Chromosome.
DR GO; GO:0005886; C:plasma 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 CDD; cd03230; ABC_DR_subfamily_A; 1.
DR Gene3D; 3.40.1710.10; abc type-2 transporter like domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR047651; ABC2_perm_RbbA.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR047817; ABC2_TM_bact-type.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; NF033858; ABC2_perm_RbbA; 1.
DR PANTHER; PTHR43038; ATP-BINDING CASSETTE, SUB-FAMILY H, MEMBER 1; 1.
DR PANTHER; PTHR43038:SF4; RIBOSOME-ASSOCIATED ATPASE; 1.
DR Pfam; PF12698; ABC2_membrane_3; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51012; ABC_TM2; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ABB67966.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 699..722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 778..800
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 867..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..231
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 260..490
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 666..892
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000259|PROSITE:PS51012"
SQ SEQUENCE 894 AA; 99012 MW; B9646F2F29330324 CRC64;
MSQHYGKTVA LNNITLDIPA RCMVGLIGPD GVGKSSLLSL ISGARVIEQG NVMVLGGDMR
DPKHRRDVCP RIAWMPQGLG KNLYHTLSVY ENVDFFARLF GHDKAEREVR INELLTSTGL
APFRDRPAGK LSGGMKQKLG LCCALIHDPE LLILDEPTTG VDPLSRAQFW DLIDSIRQRQ
SNMSVLVATA YMEEAERFDW LVAMNAGEVL ATGSAEELRQ QTQSATLEEA FINLLPQAQR
QAHQAVVIPP YQPENAEIAI EARDLTMRFG SFVAVDHVNF RIPRGEIFGF LGSNGCGKST
TMKMLTGLLP ASEGEAWLFG QPVDPKDIDT RRRVGYMSQA FSLYNELTVR QNLELHARLF
HIPEAEIPAR VAEMSERFKL NDVEDVLPES LPLGIRQRLS LAVAVIHRPE MLILDEPTSG
VDPVARDMFW QLMVDLSRQD KVTIFISTHF MNEAERCDRI SLMHAGKVLA SGTPQELVEK
RGAASLEEAF IAYLQEAAGQ SNEAEAPPVV HDTTHAPRQG FSLRRLFSYS RREALELRRD
PVRSTLALMG TVILMLIMGY GISMDVENLR FAVLDRDQTV SSQAWTLNLS GSRYFIEQPP
LTSYDELDRR MSAGDITVAI EIPPNFGRDI ARGTPVELGV WIDGAMPSRA ETVKGYVQAM
HQSWLQDVAS RQSTPASQSG LMNIETRYRY NPDVKSLPAI VPAVIPLLLM MIPSMLSTLS
VVREKELGSI INLYVTPTTR SEFLLGKQLP YIALGMLNFF LLCGLSVFVF GVPHKGSFLT
LTLAALLYII IATGMGLLIS TFMKSQIAAI FGTAIITLIP ATQFSGMIDP VASLEGPGRW
IGEVYPTSHF LTIARGTFSK ALDLTDMWQL FIPLLIAIPL VMGLSILLLK KQEG
//
