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Database: UniProt
Entry: C7MF92_BRAFD
LinkDB: C7MF92_BRAFD
Original site: C7MF92_BRAFD 
ID   C7MF92_BRAFD            Unreviewed;       992 AA.
AC   C7MF92;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Atrophied bacterial Ig domain-containing protein {ECO:0000259|Pfam:PF20578};
GN   OrderedLocusNames=Bfae_01100 {ECO:0000313|EMBL:ACU83992.1};
OS   Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG
OS   19847 / NBRC 14762 / NCIMB 9860 / 6-10).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU83992.1, ECO:0000313|Proteomes:UP000001919};
RN   [1] {ECO:0000313|EMBL:ACU83992.1, ECO:0000313|Proteomes:UP000001919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 /
RC   NCIMB 9860 / 6-10 {ECO:0000313|Proteomes:UP000001919};
RX   PubMed=21304631; DOI=10.4056/sigs.492;
RA   Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA   Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Brachybacterium faecium type strain
RT   (Schefferle 6-10).";
RL   Stand. Genomic Sci. 1:3-11(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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DR   EMBL; CP001643; ACU83992.1; -; Genomic_DNA.
DR   RefSeq; WP_012803768.1; NC_013172.1.
DR   RefSeq; YP_003153582.1; NC_013172.1.
DR   AlphaFoldDB; C7MF92; -.
DR   STRING; 446465.Bfae_01100; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   KEGG; bfa:Bfae_01100; -.
DR   PATRIC; fig|446465.5.peg.107; -.
DR   eggNOG; COG5492; Bacteria.
DR   HOGENOM; CLU_010992_0_0_11; -.
DR   OMA; REWNDIR; -.
DR   OrthoDB; 9758923at2; -.
DR   Proteomes; UP000001919; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08983; GH43_Bt3655-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR046780; aBig_2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF3; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE A-RELATED; 1.
DR   Pfam; PF20578; aBig_2; 2.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001919};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..45
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           46..992
FT                   /note="Atrophied bacterial Ig domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002980028"
FT   DOMAIN          297..361
FT                   /note="Atrophied bacterial Ig"
FT                   /evidence="ECO:0000259|Pfam:PF20578"
FT   DOMAIN          376..464
FT                   /note="Atrophied bacterial Ig"
FT                   /evidence="ECO:0000259|Pfam:PF20578"
FT   REGION          768..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  104860 MW;  EB43696309BD25F2 CRC64;
     MNTPSADGAR SPSRLRPRPA RLARAALACV LAITPAALVM PAAGAVDVPR PTAHYDMSHS
     GDILLDASGN GRDATLTGAE ESSFVTAGED EVLRFRDDVY ASLPQGLVSG DDDDFAVELT
     VSSQSDRDQF GWVIGDGIGS WNSPELGDHL FVNPRSSQSG FDGQVLAGLR AKTGEDNGEL
     RLPAGGGIGD GVATITLVGE GGELTLFLDG EEVSSLAHEH RLADIVPSGD VLGYLGRSLY
     SGDQMLEADV TDVKFWDEAL TEAQVRASQP TAAEKAATSE GLLKLDIEQA VLGKNPGLDQ
     ITGPVRLPQE MNGIALTWTS SDETVIALDG TVSRTISADT EMRLTALTPS GSVLTFDVTV
     LAPSLSSDLE AIELPERTTE NLPLLADGPV EGADIVWESS DPSVITATNP DHVAPEAGMD
     DPFAGAGVLT RPSYGAGDVD VTLTATASLG ELTETRKYTV TVAEKPRTAP DAGYAAAYFR
     SDSDERVYAA ATTENDFFTF EEVNDGAPVV SNEADTTGHR DPYILRSHEG DKYYMIATDL
     CIGCGTDWGD AQSNGSLKVN VWESTDMVHW ERTNGDDNGA ITVNQPEAGM TWAPEAYWDD
     DLQSYVLFFA SRLYDDVDHT SGEGHAQMFA VLTRDFTTFT APPSSWQDTG HARIDSTVQK
     IGDYYYRFTK NEAGDAADGL ERGKDIFLER SKVLTAPTTA SAWDADPETT WQLVDTAMTT
     PVTGHHGEGP QILALNEGDP NNTPDDDGYV FLVDNYSAGG YRAFTTSGSE ISASRQDQRL
     SQQDGWEPRT DGLPESPRHG AFVSASQQVL DAMHGWQEVK AVPSRTSLRL EGRSAIAEVA
     AEDGGDVAGP VVFSGKDWTE TVELSDGSAS AHVPEDAGEI TASYQGYRDG LVEPSSSEPL
     DVDEAQPLAT SAVPRCVAGS VTLAVTTTND GDESMKATIV TQFGSSSGVS LQPGTSTTTA
     FSTRAPEVTA GEVTVTAAGE EATASYPAAS CG
//
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