POTA_MESH2
ID POTA_MESH2 Reviewed; 444 AA.
AC Q5ZZZ7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Spermidine/putrescine import ATP-binding protein PotA {ECO:0000255|HAMAP-Rule:MF_01726};
DE EC=7.6.2.11 {ECO:0000255|HAMAP-Rule:MF_01726};
GN Name=potA {ECO:0000255|HAMAP-Rule:MF_01726}; OrderedLocusNames=mhp559;
OS Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=295358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232;
RX PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA Mahairas G.G.;
RT "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT swine mycoplasmosis.";
RL J. Bacteriol. 186:7123-7133(2004).
CC -!- FUNCTION: Part of the ABC transporter complex PotABCD involved in
CC spermidine/putrescine import. Responsible for energy coupling to the
CC transport system. {ECO:0000255|HAMAP-Rule:MF_01726}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP
CC + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.;
CC EC=7.6.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01726};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PotA),
CC two transmembrane proteins (PotB and PotC) and a solute-binding protein
CC (PotD). {ECO:0000255|HAMAP-Rule:MF_01726}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01726};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01726}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC Spermidine/putrescine importer (TC 3.A.1.11.1) family.
CC {ECO:0000255|HAMAP-Rule:MF_01726}.
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DR EMBL; AE017332; AAV27957.1; -; Genomic_DNA.
DR RefSeq; WP_011206392.1; NC_006360.1.
DR AlphaFoldDB; Q5ZZZ7; -.
DR SMR; Q5ZZZ7; -.
DR STRING; 295358.mhp559; -.
DR EnsemblBacteria; AAV27957; AAV27957; mhp559.
DR KEGG; mhy:mhp559; -.
DR eggNOG; COG3839; Bacteria.
DR HOGENOM; CLU_000604_1_1_14; -.
DR OMA; IRQKMQV; -.
DR PhylomeDB; Q5ZZZ7; -.
DR Proteomes; UP000006822; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0015417; F:ABC-type polyamine transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013611; Transp-assoc_OB_typ2.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08402; TOBE_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51305; POTA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Translocase;
KW Transport.
FT CHAIN 1..444
FT /note="Spermidine/putrescine import ATP-binding protein
FT PotA"
FT /id="PRO_0000286256"
FT DOMAIN 11..332
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT REGION 111..201
FT /note="Insert"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
SQ SEQUENCE 444 AA; 51689 MW; 140282CC71B5AF7E CRC64;
MKNIEKSEII ISLVDVDKEF GDKKVLDQIN LDIKRGDFVT LLGPSGSGKT TILRLIGGFE
WTTRGEIKFN GIDIKDVPAH KRDTATIFQD YALFPHLSVR GNIEFGLKLK RIKKKAEEIP
DVVWKKFEHL KKKWQDKQKR KIKELKILQA HLEKLLENPQ LDIKKRKKLQ DKLDDSDFRY
SNWENYLTSK SESFKKKYLT RRITKQEINK EITDIIDLVG LTGNENRAIS ELSGGMKQRV
ALARSLVIEP EIVLLDEPLS ALDTKIRQKM QVFLKKIQQK LGLTFIFVTH DQDEALQLSD
KIAIIRNGKI AQYDEPKQIY DYPVNKWVAN FIGDSNFFQA KYIKKNQVEI LGLKLYTIHD
EFIPGQKLDC LIRPEDIDID LNSGYFKGKV IQNIYKGSYY SLDIKVENTI INVETNDFYD
LETQVFIKWD DDAIHLMEME NAEI