ID A0A0R2RLK0_9PROT Unreviewed; 380 AA.
AC A0A0R2RLK0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phosphate transport system permease protein {ECO:0000256|RuleBase:RU363054};
DE Flags: Fragment;
GN ORFNames=ABS03_00650 {ECO:0000313|EMBL:KRO63447.1};
OS Pelagibacteraceae bacterium BACL5 MAG-120820-bin39.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=1655605 {ECO:0000313|EMBL:KRO63447.1, ECO:0000313|Proteomes:UP000051468};
RN [1] {ECO:0000313|EMBL:KRO63447.1, ECO:0000313|Proteomes:UP000051468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL5 MAG-120820-bin39 {ECO:0000313|EMBL:KRO63447.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the binding-protein-dependent transport system for
CC phosphate; probably responsible for the translocation of the substrate
CC across the membrane. {ECO:0000256|RuleBase:RU363054}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|RuleBase:RU363054}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|RuleBase:RU363054}. Cell membrane
CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363032}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000256|RuleBase:RU363054}.
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:KRO63447.1}.
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DR EMBL; LIBV01000193; KRO63447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2RLK0; -.
DR Proteomes; UP000051468; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR InterPro; IPR011864; Phosphate_PstC.
DR NCBIfam; TIGR02138; phosphate_pstC; 1.
DR PANTHER; PTHR42727; PHOSPHATE TRANSPORT SYSTEM PERMEASE PROTEIN; 1.
DR PANTHER; PTHR42727:SF1; PHOSPHATE TRANSPORT SYSTEM PERMEASE-RELATED; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|RuleBase:RU363054};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW Phosphate transport {ECO:0000256|RuleBase:RU363054};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363032};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363032};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363032}.
FT TRANSMEM 39..60
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 80..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 148..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 232..250
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 280..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 350..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 152..368
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRO63447.1"
SQ SEQUENCE 380 AA; 41257 MW; 36485B922057E522 CRC64;
NAANLLYEKV KSIYSGNFFG DIDFVLKESA VSYAKFLNLF TNSKIVLVFT LIIASIIYSL
KKIKNNNKAR DDVEFILKGL LFTSSLIAIL TTIGIIFSLL FESIKFFSVI NVFDYLFGTN
WSPQRAFVRD ATTITAAEYE ELKDAFGFIP LIAGTAFIAL IAMLVAVPIG LFSGIYMAEY
ASIKVRKFSK PIIEILAGIP TVVYGFFAAL TVGPFFRELG ESLGLTVSSE SALAAGLIMG
IMIIPYISSL SDDVINSVPQ SLRDASYAIG ATQSETIKKV VIPAALPGII GSILLAVSRA
IGETMIVVMA AGLAANLTIN PLDSTTTITT QIVMILVGDQ EFNSPKTQSA FALGLTLFIA
TLILNYIALR VVKKYREKYE
//
