ID I0SWH8_STRMT Unreviewed; 521 AA.
AC I0SWH8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=ABC transporter, permease protein {ECO:0000313|EMBL:EID27731.1};
GN ORFNames=HMPREF1048_0955 {ECO:0000313|EMBL:EID27731.1};
OS Streptococcus mitis SK575.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1095736 {ECO:0000313|EMBL:EID27731.1, ECO:0000313|Proteomes:UP000005505};
RN [1] {ECO:0000313|EMBL:EID27731.1, ECO:0000313|Proteomes:UP000005505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK575 {ECO:0000313|EMBL:EID27731.1,
RC ECO:0000313|Proteomes:UP000005505};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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:EID27731.1}.
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DR EMBL; AICU01000076; EID27731.1; -; Genomic_DNA.
DR RefSeq; WP_001227317.1; NZ_AICU01000076.1.
DR AlphaFoldDB; I0SWH8; -.
DR PATRIC; fig|1095736.3.peg.1307; -.
DR OrthoDB; 9811552at2; -.
DR Proteomes; UP000005505; Unassembled WGS sequence.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0071705; P:nitrogen compound transport; IEA:InterPro.
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; 2.
DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR InterPro; IPR043429; ArtM/GltK/GlnP/TcyL/YhdX-like.
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; PTHR30614:SF20; GLUTAMINE TRANSPORT SYSTEM PERMEASE PROTEIN GLNP; 1.
DR PANTHER; PTHR30614; MEMBRANE COMPONENT OF AMINO ACID ABC TRANSPORTER; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
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 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..521
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003634642"
FT TRANSMEM 297..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 474..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 297..496
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
SQ SEQUENCE 521 AA; 57435 MW; 2376CAE37E633ACA CRC64;
MRKIYLSIFT SLLLMLGLVN VAQADEYLRI GMEAAYAPFN WTQDDDSNGA VKIDGTNQYA
NGYDVQIAKK IAKDLGKEPL VVKTKWEGLV PALTSGKIDM IIAGMSPTAE RKQEIAFSSS
YYTSEPVLLV KKDSTYANAK SLDDFNGAKI TSQQGVYLYD LIAQISGAKK ETAMGDFAQM
RQALEAGVID AYVSERPEAL TAEAANSKFK MVQVEPGFKT GEEDTAIAIG LRKDDNRISQ
INASIETISK DDQVALMDRM IKEQPAEATT TEETSSSFFS QVAKILSENW QQLLRGAGIT
LLISIVGTII GLIIGLAIGV FRTAPLSENK VIYGLQKLVG WILNVYIEIF RGTPMIVQSM
VIYYGTAQAF GINLDRTLAA IFIVSINTGA YMTEIVRGGI LAVDKGQFEA ATALGMTHNQ
TMRKIVLPQV VRNILPATGN EFVINIKDTS VLNVISVVEL YFSGNTVATQ TYQYFQTFTI
IAVIYFVLTF TVTRILRFIE RRMDMDTYTT GANQMQTEDL K
//