ID A0A090E252_9BACT Unreviewed; 337 AA.
AC A0A090E252;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ABC-type transporter, substrate-binding protein {ECO:0000313|EMBL:CDR34744.1};
GN ORFNames=CSEC_1937 {ECO:0000313|EMBL:CDR34744.1};
OS Criblamydia sequanensis CRIB-18.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Criblamydiaceae;
OC Criblamydia.
OX NCBI_TaxID=1437425 {ECO:0000313|EMBL:CDR34744.1, ECO:0000313|Proteomes:UP000031552};
RN [1] {ECO:0000313|EMBL:CDR34744.1, ECO:0000313|Proteomes:UP000031552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB-18 {ECO:0000313|EMBL:CDR34744.1,
RC ECO:0000313|Proteomes:UP000031552};
RA Linke B.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDR34744.1, ECO:0000313|Proteomes:UP000031552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB-18 {ECO:0000313|EMBL:CDR34744.1,
RC ECO:0000313|Proteomes:UP000031552};
RA Bertelli C., Goesmann A., Greub G.;
RT "Criblamydia sequanensis harbors a mega-plasmid encoding arsenite
RT resistance.";
RL Submitted (SEP-2014) 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:CDR34744.1}.
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DR EMBL; CCEJ010000009; CDR34744.1; -; Genomic_DNA.
DR RefSeq; WP_053331983.1; NZ_CCEJ010000009.1.
DR AlphaFoldDB; A0A090E252; -.
DR STRING; 1437425.CSEC_1937; -.
DR eggNOG; COG0803; Bacteria.
DR OrthoDB; 9793396at2; -.
DR Proteomes; UP000031552; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
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 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000031552};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003512}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..337
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001854510"
SQ SEQUENCE 337 AA; 38390 MW; 4C579813B4FD1DB6 CRC64;
MRLIRAFSFI VLLICSFSCA QNNSRQNDLK KWFESNGKIK ILTTTRMIHD LVKEIGGDKV
DTLPLIIGEL DPHSYQLVKG DDEKIARADL IFFNGLNLEH GPSLKQLLYE KKNAYAIGDY
LKETHPEEVL YLGKEVDPHI WMDVSLFAKT IPVITEALSK QDPANKEFYK ERSFNLEKEL
KELHLSVKNI LHEVPEEKRY LVTSHDAFNY FARAYLATDE EVKTGSWSKR FQAPEGLAPD
SQLSLQDINF IINHLRTYNI EVIFPESNVS QNSLKKIVEA IEAKGGVIRI ANCSLYADAM
GKEGSRGDSY LKMLRYDAEL IASNLFPQKG GILKCNE
//