ID A0A147ECI9_9MICO Unreviewed; 454 AA.
AC A0A147ECI9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cell wall-binding protein {ECO:0000313|EMBL:KTR81879.1};
GN ORFNames=NS354_11855 {ECO:0000313|EMBL:KTR81879.1};
OS Leucobacter chromiiresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR81879.1, ECO:0000313|Proteomes:UP000070810};
RN [1] {ECO:0000313|EMBL:KTR81879.1, ECO:0000313|Proteomes:UP000070810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS354 {ECO:0000313|EMBL:KTR81879.1,
RC ECO:0000313|Proteomes:UP000070810};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTR81879.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDRK01000110; KTR81879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A147ECI9; -.
DR PATRIC; fig|1079994.3.peg.277; -.
DR Proteomes; UP000070810; Unassembled WGS sequence.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF270; OUTER MEMBRANE ANTIGENIC LIPOPROTEIN B; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000070810};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..454
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007544203"
FT DOMAIN 348..438
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT REGION 165..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..123
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 165..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 47578 MW; C38C2934CDFFA125 CRC64;
MQKRKASTTR RVLGVFAACA IGAGMLVGAQ FNAPPAQALD LPTWDDVQQA KQNQSTAAKK
VTEIESLIAE GEKELDRLRN LHATTIDELH EAEDALAAAS EKAANLETQA EASRKEADEA
ADRAGAIVAQ MYRSGGVDRS VEMFLDSDGS TADALLDRMA SMSKATERNT TLSQEAEQAA
NTADTLGKQA EAAAQEREEL RQVQEEKEAA AAEAVAGQGD KVRKQEEQQK TLQTQLAALK
DTTTKTVEGY EERLRIEEEQ RRAEAERLRK EAEAARKAAE EEAARRAAAG GGGGGGGAPA
PGGGGGGGGG GSAPPPSGGG GGGSNGWIYP TAGFYVSEGF RPPGRPDHTG IDLATGCGTP
IFAAKEGTVA LAYWDGGGGG NMVSINHPNG WQTRYAHMIG WATVSAGQQV SAGQVVGYVG
NTGASTGCHL HFEMRPNQDN GWYDFVNPAW YIAF
//
