ID A0A0G3ACF1_9ACTN Unreviewed; 1193 AA.
AC A0A0G3ACF1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Sodium/proline symporter {ECO:0000256|RuleBase:RU366012};
DE AltName: Full=Proline permease {ECO:0000256|RuleBase:RU366012};
GN ORFNames=ABB07_01260 {ECO:0000313|EMBL:AKJ08714.1};
OS Streptomyces incarnatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ08714.1, ECO:0000313|Proteomes:UP000035366};
RN [1] {ECO:0000313|EMBL:AKJ08714.1, ECO:0000313|Proteomes:UP000035366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX PubMed=26159526;
RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA Tamura T.;
RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT the Nucleoside Antibiotic Sinefungin.";
RL Genome Announc. 3:e00715-e00715(2015).
CC -!- FUNCTION: Catalyzes the sodium-dependent uptake of extracellular L-
CC proline. {ECO:0000256|RuleBase:RU366012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out);
CC Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039;
CC Evidence={ECO:0000256|ARBA:ARBA00033708};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU366012};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU366012}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000256|ARBA:ARBA00006434, ECO:0000256|RuleBase:RU366012}.
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DR EMBL; CP011497; AKJ08714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3ACF1; -.
DR STRING; 665007.ABB07_01260; -.
DR PATRIC; fig|665007.5.peg.300; -.
DR Proteomes; UP000035366; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005298; F:proline:sodium symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031402; F:sodium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015824; P:proline transport; IEA:UniProtKB-UniRule.
DR CDD; cd16936; HATPase_RsbW-like; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd11475; SLC5sbd_PutP; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR011851; Na/Pro_symporter.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR NCBIfam; TIGR02121; Na_Pro_sym; 1.
DR NCBIfam; TIGR00813; sss; 1.
DR PANTHER; PTHR48086; SODIUM/PROLINE SYMPORTER-RELATED; 1.
DR PANTHER; PTHR48086:SF3; SODIUM_PROLINE SYMPORTER; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR Pfam; PF00474; SSF; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 3: Inferred from homology;
KW Amino-acid transport {ECO:0000256|RuleBase:RU366012};
KW Cell membrane {ECO:0000256|RuleBase:RU366012};
KW Ion transport {ECO:0000256|RuleBase:RU366012};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU366012};
KW Sodium {ECO:0000256|RuleBase:RU366012};
KW Sodium transport {ECO:0000256|RuleBase:RU366012};
KW Symport {ECO:0000256|RuleBase:RU366012};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU366012};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU366012};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366012}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 69..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 128..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 159..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 241..263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 291..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 332..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 403..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 431..450
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT TRANSMEM 462..486
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366012"
FT DOMAIN 624..813
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT DOMAIN 834..1061
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|SMART:SM00331"
SQ SEQUENCE 1193 AA; 127110 MW; FA7193F345AFC9A0 CRC64;
MFDVSAPIVA TFLVYVAVMI GTGVWAYTRT RTFADFALGG RRLSAFVAAL SAGASDMSGW
LFLAFPGAVY AAGVGAGWIA AGLVIGTYLN WLFVAPRLRT YTERAHNAVS LSAYLEERFE
DRTRMLRMVS AAVTLVFFTV YVASGLVAGG LLFGHIFGVG FGLGVALTAL VIVVYSCLGG
FLAVSLTHVL QATLMFLALL VLPAVAIGAL GGFGTLRDTL NRKTPSLLDM GARVDLTGGR
WTAGGSLGAV AIVSLLAWGL GYFGQPHILA RFMGIRSTGA IPTARRIETG WVIIVLAGAM
LVGLVGIAQT GAPLHDPQTV YISLSRSLLN PWGAGVMLIA VLAAIISTAD SQLLVSSVAL
TEDFYRAFLH RRASDRTLIW AGRAAVIAVT LVAFAIALRG GGLLGIVAYA WAGFGAAFGP
VVLLSLYWPR MTWAGAMAGI VSGAATVLLW KRINPLLGPF QSGIYEMVPG VLIATAAALV
FGRFVGRPPK RAFWRMPGGG VSQLMLTPFL SHAPVGIAVL DTDLRYVWVN EPLDRQIPLE
RRLGRRMAEV LPEQEAAAFE EKMRGVLRTG TPVMDFEYRG AGHRDPDAGR AVSASFFAMK
DRHGRNVGVW YMVIDVTERW RAQQRLALLN DAATRIGSTL DVTRTAQELA DDAVPAVADF
VAVDLLDSVM RGEEPAPGPV GMSPVIRRAA QQSVRAGCPE AALAVGETVR RAPASPVTRC
LLESRTLVER ILDRTNSPWV TEDETLGASL LDYDFRSVMV IPVRARGVTL GAATFARSRR
LGPFEEDDVR LAEELVSRAA VCIDNARRFT RERTAARSMQ RYLLPQDPTG GSALEVASWY
LPTDAPSGVG GDWFDVIPLS GARVALVVGD VAGHGIHAAA TMGRLRTAVR TLANLDLPPD
ELLAHLDDLV IGLMASSDSD APPAGEGAAA GTAFMGATCL YAVYDPVSGR CTLARAGHLP
PMIIGPHGGA DIVDLPAGPP LGLGYLPFES AELELPEGSL IALYTDGLIE SVDQDIDAGL
SRLGAVLAGP WPTLEETGRR VIEDLTAKPP ADDAALILAR TRVLARDRVV TWNLPSDPAA
VAHARSLATQ QLQEWGIPDL TFTTELIVSE LVTNAIRHAT GPVCLRLIRD RALICEVSDA
SSTSPRLRHA RTTDEGGRGL LIVAQLARRW GTRYTATGKI IWTEQAVPGD PDT
//