ID B2IM73_STRPS Unreviewed; 521 AA.
AC B2IM73;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Amino acid ABC transporter, amino acid-binding protein/permease protein {ECO:0000313|EMBL:ACB89700.1};
GN Name=glnH {ECO:0000313|EMBL:ACB89700.1};
GN OrderedLocusNames=SPCG_0448 {ECO:0000313|EMBL:ACB89700.1};
OS Streptococcus pneumoniae (strain CGSP14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=516950 {ECO:0000313|EMBL:ACB89700.1, ECO:0000313|Proteomes:UP000001682};
RN [1] {ECO:0000313|EMBL:ACB89700.1, ECO:0000313|Proteomes:UP000001682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGSP14 {ECO:0000313|EMBL:ACB89700.1,
RC ECO:0000313|Proteomes:UP000001682};
RX PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT "Genome evolution driven by host adaptations results in a more virulent and
RT antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL BMC Genomics 10:158-158(2009).
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; CP001033; ACB89700.1; -; Genomic_DNA.
DR RefSeq; WP_001227307.1; NC_010582.1.
DR AlphaFoldDB; B2IM73; -.
DR SMR; B2IM73; -.
DR GeneID; 66805641; -.
DR KEGG; spw:SPCG_0448; -.
DR HOGENOM; CLU_019602_20_4_9; -.
DR Proteomes; UP000001682; Chromosome.
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_5002776730"
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; 57359 MW; 4E940E1DA1502501 CRC64;
MRKIYLSIFT SLLLMLGLVN VAQADEYLRI GMEAAYAPFN WTQDDDSNGA VKIDGTNQYA
NGYDVQIAKK IAKDLGKEPL VVKTKWEGLV PALTSGKIDM IIAGMSPTAE RKQEIAFSSS
YYTSEPVLLV KKDSAYASAK SLDDFNGAKI TSQQGVYLYD LIAQIPGAKK ETAMGDFAQM
RQALEAGVID AYVSERPEAL TAEAANSKFK MIQVEPGFKT GEEDTAIAIG LRKNDNRISQ
INASIETISK DDQVALMDRM IKEQPAEATT TEETSSSFFS QVAKILSENW QQLLRGAGIT
LLISIVGTII GLIIGLAIGV FRTAPLSENK AIYGLQKLVG WVLNVYIEIF RGTPMIVQSM
VIYYGTAQAF GINLDRTLAA IFIVSINTGA YMTEIVRGGI LAVDKGQFEA ATALGMTHNQ
TMRKIVLPQV VRNILPATGN EFVINIKDTS VLNVISVVEL YFSGNTVATQ TYQYFQTFTI
IAVIYFVLTF TVTRILRFIE RRMDMDTYTT GANQMQTEDL K
//
