ID K9EWL5_9ACTO Unreviewed; 362 AA.
AC K9EWL5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Metal ABC transporter substrate-binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9233_00707 {ECO:0000313|EMBL:EKU95342.1};
OS Actinobaculum massiliense ACS-171-V-Col2.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=883066 {ECO:0000313|EMBL:EKU95342.1, ECO:0000313|Proteomes:UP000009888};
RN [1] {ECO:0000313|EMBL:EKU95342.1, ECO:0000313|Proteomes:UP000009888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-171-V-Col2 {ECO:0000313|Proteomes:UP000009888};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinobaculum massiliae ACS-171-V-COL2.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC {ECO:0000256|RuleBase:RU003512}.
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:EKU95342.1}.
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DR EMBL; AGWL01000003; EKU95342.1; -; Genomic_DNA.
DR AlphaFoldDB; K9EWL5; -.
DR STRING; 202789.GCA_001457435_01424; -.
DR PATRIC; fig|883066.3.peg.726; -.
DR eggNOG; COG0803; Bacteria.
DR HOGENOM; CLU_016838_1_1_11; -.
DR Proteomes; UP000009888; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR CDD; cd01137; PsaA; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR InterPro; IPR006129; AdhesinB.
DR InterPro; IPR006128; Lipoprotein_PsaA-like.
DR InterPro; IPR006127; ZnuA-like.
DR PANTHER; PTHR42953; HIGH-AFFINITY ZINC UPTAKE SYSTEM PROTEIN ZNUA-RELATED; 1.
DR PANTHER; PTHR42953:SF1; MANGANESE ABC TRANSPORTER SUBSTRATE-BINDING LIPOPROTEIN; 1.
DR Pfam; PF01297; ZnuA; 1.
DR PRINTS; PR00691; ADHESINB.
DR PRINTS; PR00690; ADHESNFAMILY.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009888};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003512}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..362
FT /note="Metal ABC transporter substrate-binding protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038695874"
FT REGION 308..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 38442 MW; 1D9C301A589E376B CRC64;
MLKQTRRFSR AAAILAALML IVAGCSPRSV SHSANANNDD RPLVLTSFTV IADMAKNVGG
DLVRVESITV PGAEIHDFQP SPEDIKRGEG ADLILYNGLG LERWFEKYVE NSSAKVAVLS
DGIEAMPIAA GDYAGAPNPH AWMSPANGKI YVDNIVRALS DLDPDNSATY EKNGAAYKEK
LDEISTEMNQ QLSALPESQR ALVTCEGAFS YLTRDQGMQE RYLWAVNAEG AQSPRAKAEL
ENFVRESGVK SLFCETTVDD KMASVSEDTG VPVAGLLYVD SLSDADGPVP TYLDLLRYDA
DLITSGLRGE SSAGQAGKEP SAPPSEHSAD SSAGSAHADN SADSSSDGTT PDNSEQKDGT
NG
//
