ID A0A200H711_9ACTN Unreviewed; 1348 AA.
AC A0A200H711;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|PROSITE:PS50853};
GN ORFNames=BHE97_13730 {ECO:0000313|EMBL:OUZ08284.1};
OS Aeromicrobium sp. PE09-221.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1898043 {ECO:0000313|EMBL:OUZ08284.1, ECO:0000313|Proteomes:UP000195423};
RN [1] {ECO:0000313|EMBL:OUZ08284.1, ECO:0000313|Proteomes:UP000195423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PE09-221 {ECO:0000313|EMBL:OUZ08284.1,
RC ECO:0000313|Proteomes:UP000195423};
RX PubMed=28218694;
RA Matobole R.M., van Zyl L.J., Parker-Nance S., Davies-Coleman M.T.,
RA Trindade M.;
RT "Antibacterial Activities of Bacteria Isolated from the Marine Sponges
RT Isodictya compressa and Higginsia bidentifera Collected from Algoa Bay,
RT South Africa.";
RL Mar. Drugs 15:E47-E47(2017).
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:OUZ08284.1}.
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DR EMBL; MIJB01000025; OUZ08284.1; -; Genomic_DNA.
DR Proteomes; UP000195423; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:InterPro.
DR CDD; cd00063; FN3; 6.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR InterPro; IPR013486; SpoIID/LytB.
DR InterPro; IPR013693; SpoIID/LytB_N.
DR NCBIfam; TIGR02669; SpoIID_LytB; 1.
DR PANTHER; PTHR46708:SF2; SUBSTRATE-ADHESION MOLECULE; 1.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF08486; SpoIID; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR PROSITE; PS50853; FN3; 6.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000195423};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1348
FT /note="Fibronectin type-III domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039143926"
FT DOMAIN 441..527
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 528..614
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 617..703
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 704..790
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 796..882
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 888..974
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 31..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1348 AA; 142469 MW; ACC9FC95DD727580 CRC64;
MHSRLLSLRS AAALLISLLL VLVAFEPAAA EPTPAVPPAG TATTAPVEAE ESPAPVEEQP
PAESSEPQVE EAPSTPVEGA PSADAPILGA LQAERVDDGA LSDLVTVENV EVPEDTLRAL
SATDDSILEK VDLSPFHMAA VSWDPEAEAT GVSIVMSVRV AGEWTEWEDL ALADGEGSPS
ASDPLWTSEP ADGVRARVTS DQGALPDLKI TTVDPGPEDV ATPEGGGAGQ LTGLASVAQP
AIITRAGWGA GPGQRCDATR GSMRSVVIHH TAGANSYSKA QSAGIVRSYQ TMHIVTNGWC
DIGYNFLVDK YGQIFEGRAG SIAGHRRGAH AGVGAVNDNS TGIAMMGNFE SANIWNGEWG
TLRSTVSRLT AWRLQRFGLK PLTQVTLAGR TNFTVNGHRN WTATACPGRY GLDWLNAGNG
LRADVDKLMH SSPPKPTRLG TPTGLNLSSV GESNLSLAWA GVGGATSYRV KWGENSPNDN
ARTVSGTRVD LTGLKPGTTY RVVIAASAPG AIQSYFSKEH TFTTRLATPT GLTSVASTND
SLSLSWGKVP QATSYRVKWG ENSPNDNART VSGTRVDLTG LKPGTTYRVV IAASAPGAAQ
SYFTKEHTFT VGGRLATPTG FKLNSSGVSN LNLSWTGVGG AATYRVKWGE KSPNDNSRDV
SGTRVDLTGL KPGTTYRVVI AARAPGATQS YFSKEHTFTT RLATPTGLTS VASTNDSLSL
SWGKVPQATS YRVKWGENSP NDNARTVSGT RVNLTGLKPG TTYRVVIAAS APGATQSYFS
KEHTFTTQNA SGRLATPTGL KLSSVGETSL NLSWTGVGGA ATYRVKWGEN SPNDNSRDVS
GTSVNLTGLK PGTTYRVVIA ARAPGATQSY FSKEHTFTTK NFSGRLATPT GLKLTSSTVN
TLGLSWTTVP YATNYRVKWG EGSPNSNTRD ISGTTISLTG LKPGTTYRVV IAARAPGATQ
SYFSKEHTFT TKANSSNSAT FSNGSVTMKG HGYGHGVGMS QYGAQGGALA GRTFQQILSH
YYPGTTLATR NAKIRVQISG APTDALTVRP KSGLMVQSAG GGPNKVLPAR PDGRHVDLWQ
VVRAGDSSRN QLRYNTGGRW HNHGGTWRGD VQFGVDGGTV TALFGSQDRT FRGVIRWWTG
SGSARTTVNE LFSLDDYIRG VVPREMPSGW HQQALRSQAV AARTYALRTM NPGRADYDIC
DTTACQVYGA VSAEAVTTNT AIDATRGQVL MYNGTPAFTQ YSSSSGGYTN WPSYPRDHPY
LKPVKDDWDA VSSNPNHSWT TTLTADAVRR AYPQIGTPRT IQVTARNGYG AMGGRVDKVR
ITGSGGSVEV TGNGARTAFG LKSNWFGF
//