ID F5X257_STRPX Unreviewed; 739 AA.
AC F5X257;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Polar amino acid transport system permease/substrate-binding protein {ECO:0000313|EMBL:BAK30366.1};
GN OrderedLocusNames=SGPB_1319 {ECO:0000313|EMBL:BAK30366.1};
OS Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK30366.1, ECO:0000313|Proteomes:UP000007946};
RN [1] {ECO:0000313|EMBL:BAK30366.1, ECO:0000313|Proteomes:UP000007946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC {ECO:0000313|Proteomes:UP000007946};
RX PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA Chang C.-H., Hsu M.-T.;
RT "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL PLoS ONE 6:E20519-E20519(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363032};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000256|RuleBase:RU363032}.
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DR EMBL; AP012054; BAK30366.1; -; Genomic_DNA.
DR RefSeq; WP_013852035.1; NC_015600.1.
DR AlphaFoldDB; F5X257; -.
DR STRING; 981540.SGPB_1319; -.
DR KEGG; stb:SGPB_1319; -.
DR HOGENOM; CLU_019602_20_0_9; -.
DR Proteomes; UP000007946; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0071705; P:nitrogen compound transport; IEA:InterPro.
DR CDD; cd13619; PBP2_GlnP; 1.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR InterPro; IPR001320; Iontro_rcpt_C.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR01726; HEQRo_perm_3TM; 1.
DR PANTHER; PTHR35936:SF17; GLUTAMINE-BINDING PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR SMART; SM00062; PBPb; 2.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW Reference proteome {ECO:0000313|Proteomes:UP000007946};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..739
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038396380"
FT TRANSMEM 540..562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 574..595
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 712..731
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 536..731
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
SQ SEQUENCE 739 AA; 80078 MW; 5264A0681DD28F94 CRC64;
MKHKLKALML AIFSVFFVFG VKAQADTISI VSDTAYAPFE FKDSDQTYKG IDVDIIKEVA
KREGWDYEQT YPGFDAAVNA VQAGQADALM AGTTVTDARK KVFTFSDTYY DTSIVIYTKS
GNTAISKYSQ LKGKTVGVKN GTAAQTWLDE HADKYGYTVK TFDTSDLMNN SLDSGSIDAA
MDDTPVVQYA INQGKSYEIN IDAESIGSFA FAVKKGSSYE YLIDEFNEAL AAMKEDGTYD
QIMQKWLGDS YTSSSTSSSS NSSAASSTLT LTGDASAKAT PVKSTYKIVM DSSFAPFEYQ
NDSGEYEGID VELIKAIAEQ QGFNVEISNP GFDAALNAVQ AGQADAVIAG MSITDARKEI
FDFSDAYYTS NILLAVKSGS SVKSYSDLKG LTVGAKNGTS SYTWLSEHAD EYGYTLKAFD
EASTMYDSLN SGSIDALMDD EAVLLYAIQQ GRDFETPIAG EKSGEYGFAV SKGSNPELIE
MFNNGLAALV ESGEYDEIVN KYLDTSDSSS SSSSTVDETT IWGLLKNNYS QLLAGLGKTL
SLTLISFAIA MVIGIIFGMM AVAPNKVLRT ISAVFVDIVR GIPLMIVAAF IFWGIPNLLE
SITGRQSPIN DFVAATIALS LNGGAYIAEI VRGGIEAVPQ GQMEASRSLG ISYGKTMQKI
ILPQAIRLML PNFINQFVIS LKDTTIVSAI GLVELFQTGK IIIARNYQSF RVYAILAVIY
LVMITLLTRL AKRLEKRLK
//